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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 //