ACFD_ECOLI
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 03-AUG-2022, entry version 61.
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 AlphaFoldDB; P0CK95; -.
DR BioGRID; 4262979; 9.
DR STRING; 511145.b4466; -.
DR MEROPS; M98.001; -.
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; COG3064; Bacteria.
DR HOGENOM; CLU_006312_0_0_6; -.
DR OMA; VMGNARY; -.
DR BioCyc; EcoCyc:G7541-MON; -.
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 REGION 22..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1498..1520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..87
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1506..1520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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
