ID   ACFD_ECOLI              Reviewed;        1520 AA.
AC   P0CK95; Q2M9M2; Q46837; Q46838; Q6BF58;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 1.
DT   11-DEC-2019, entry version 53.
DE   RecName: Full=Putative lipoprotein AcfD homolog;
DE   Flags: Precursor;
GN   Name=yghJ; OrderedLocusNames=b4466, JW5925; ORFNames=ECK2968;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [2]
RP   SEQUENCE REVISION.
RX   PubMed=16397293; DOI=10.1093/nar/gkj405;
RA   Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA   Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA   Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA   Thomson N.R., Wishart D., Wanner B.L.;
RT   "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT   -- 2005.";
RL   Nucleic Acids Res. 34:1-9(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1321-1520.
RC   STRAIN=O15:H- / 83/39 / ETEC;
RA   Tauschek M., Gorrell R.J., Strugnell R.A., Robins-Browne R.M.;
RT   "Identification of a type II protein secretory pathway required for the
RT   secretion of heat-labile enterotoxin by enterotoxigenic Escherichia coli.";
RL   Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in a type II secretion system (T2SS, formerly
CC       general secretion pathway, GSP) for the export of folded proteins
CC       across the outer membrane. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC   -!- MISCELLANEOUS: In many other E.coli strains this gene is part of a type
CC       II secretion system, but in MG1655 the locus is missing a number of
CC       genes. {ECO:0000305}.
CC   -!- SIMILARITY: To V.cholerae AcfD (VC_0845). {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA69140.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAA69141.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U28377; AAA69141.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; U28377; AAA69140.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; U00096; AAT48156.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77034.1; -; Genomic_DNA.
DR   EMBL; AF426313; AAL60194.1; -; Genomic_DNA.
DR   RefSeq; WP_001034469.1; NZ_LN832404.1.
DR   RefSeq; YP_026189.1; NC_000913.3.
DR   BioGrid; 4262979; 9.
DR   STRING; 511145.b4466; -.
DR   MEROPS; M98.001; -.
DR   jPOST; P0CK95; -.
DR   PaxDb; P0CK95; -.
DR   PRIDE; P0CK95; -.
DR   EnsemblBacteria; AAT48156; AAT48156; b4466.
DR   EnsemblBacteria; BAE77034; BAE77034; BAE77034.
DR   GeneID; 2847716; -.
DR   KEGG; ecj:JW5925; -.
DR   KEGG; eco:b4466; -.
DR   PATRIC; fig|1411691.4.peg.3758; -.
DR   eggNOG; ENOG4105F88; Bacteria.
DR   eggNOG; ENOG410XS21; LUCA.
DR   KO; K10939; -.
DR   BioCyc; EcoCyc:G7541-MONOMER; -.
DR   PRO; PR:P0CK95; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   Gene3D; 1.10.390.30; -; 1.
DR   InterPro; IPR025385; DUF4092.
DR   InterPro; IPR035423; M60-like_N.
DR   InterPro; IPR042279; Pep_M60_3.
DR   InterPro; IPR031161; Peptidase_M60_dom.
DR   Pfam; PF13322; DUF4092; 1.
DR   Pfam; PF17291; M60-like_N; 1.
DR   Pfam; PF13402; Peptidase_M60; 1.
DR   SMART; SM01276; M60-like; 1.
DR   PROSITE; PS51723; PEPTIDASE_M60; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Lipoprotein; Membrane; Palmitate;
KW   Reference proteome; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           24..1520
FT                   /note="Putative lipoprotein AcfD homolog"
FT                   /id="PRO_0000020619"
FT   DOMAIN          1081..1381
FT                   /note="Peptidase M60"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01060"
FT   LIPID           24
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           24
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   VARIANT         1358
FT                   /note="N -> G (in strain: O15:H- / 83/39 /ETEC)"
FT   VARIANT         1392..1402
FT                   /note="DGTPLPEFYSE -> EGELPKFFSD (in strain: O15:H- / 83/39
FT                   / ETEC)"
FT   VARIANT         1423..1428
FT                   /note="EVSNDK -> DVGDKT (in strain: O15:H- / 83/39 / ETEC)"
FT   VARIANT         1498
FT                   /note="D -> K (in strain: O15:H- / 83/39 /ETEC)"
FT   VARIANT         1511
FT                   /note="Q -> K (in strain: O15:H- / 83/39 /ETEC)"
FT   VARIANT         1519
FT                   /note="A -> V (in strain: O15:H- / 83/39 /ETEC)"
SQ   SEQUENCE   1520 AA;  167246 MW;  C835E4953471A7B3 CRC64;
     MNKKFKYKKS LLAAILSATL LAGCDGGGSG SSSDTPPVDS GTGSLPEVKP DPTPNPEPTP
     EPTPDPEPTP EPIPDPEPTP EPEPEPVPTK TGYLTLGGSQ RVTGATCNGE SSDGFTFKPG
     EDVTCVAGNT TIATFNTQSE AARSLRAVEK VSFSLEDAQE LAGSDDKKSN AVSLVTSSNS
     CPANTEQVCL TFSSVIESKR FDSLYKQIDL APEEFKKLVN EEVENNAATD KAPSTHTSPV
     VPVTTPGTKP DLNASFVSAN AEQFYQYQPT EIILSEGRLV DSQGYGVAGV NYYTNSGRGV
     TGENGEFSFS WGETISFGID TFELGSVRGN KSTIALTELG DEVRGANIDQ LIHRYSTTGQ
     NNTRVVPDDV RKVFAEYPNV INEIINLSLS NGATLGEGEQ VVNLPNEFIE QFNTGQAKEI
     DTAICAKTDG CNEARWFSLT TRNVNDGQIQ GVINKLWGVD TNYKSVSKFH VFHDSTNFYG
     STGNARGQAV VNISNAAFPI LMARNDKNYW LAFGEKRAWD KNELAYITEA PSLVEPENVT
     RDTATFNLPF ISLGQVGEGK LMVIGNPHYN SILRCPNGYS WNGGVNKDGQ CTLNSDPDDM
     KNFMENVLRY LSDDKWKPDA KASMTVGTNL DTVYFKRHGQ VTGNSAAFDF HPDFAGISVE
     HLSSYGDLDP QEMPLLILNG FEYVTQVGND PYAIPLRADT SKPKLTQQDV TDLIAYLNKG
     GSVLIMENVM SNLKEESASG FVRLLDAAGL SMALNKSVVN NDPQGYPNRV RQQRATGIWV
     YERYPAVDGA LPYTIDSKTG EVKWKYQVEN KPDDKPKLEV ASWLEDVDGK QETRYAFIDE
     ADHKTEDSLK AAKEKIFAAF PGLKECTNPA YHYEVNCLEY RPGTGVPVTG GMYVPQYTQL
     SLNADTAKAM VQAADLGTNI QRLYQHELYF RTNGRKGERL SSVDLERLYQ NMSVWLWNDT
     SYRYEEGKND ELGFKTFTEF LNCYANDAYA GGTKCSADLK KSLVDNNMIY GDGSSKAGMM
     NPSYPLNYME KPLTRLMLGR SWWDLNIKVD VEKYPGAVSE EGQNVTETIS LYSNPTKWFA
     GNMQSTGLWA PAQKEVTIKS NANVPVTVTV ALADDLTGRE KHEVALNRPP RVTKTYSLDA
     SGTVKFKVPY GGLIYIKGNS STNESASFTF TGVVKAPFYK DGAWKNDLNS PAPLGELESD
     AFVYTTPKKN LNASNYTGGL EQFANDLDTF ASSMNDFYGR DSEDGKHRMF TYKNLPGHKH
     RFTNDVQISI GDAHSGYPVM NSSFSPNSTT LPTTPLNDWL IWHEVGHNAA ETPLTVPGAT
     EVANNVLALY MQDRYLGKMN RVADDITVAP EYLEESNNQA WARGGAGDRL LMYAQLKEWA
     EKNFDIKKWY PDGTPLPEFY SEREGMKGWN LFQLMHRKAR GDEVSNDKFG GKNYCAESNG
     NAADTLMLCA SWVAQTDLSE FFKKWNPGAN AYQLPGASEM SFEGGVSQSA YNTLASLDLP
     KPEQGPETIN QVTEHKMSAE
//
