ID   ACFD_ECOH1              Reviewed;        1519 AA.
AC   E3PJ90; Q2M9M2; Q46837; Q46838; Q6BF58;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Putative lipoprotein YghJ;
DE   AltName: Full=Putative lipoprotein AcfD homolog;
DE   Flags: Precursor;
GN   Name=yghJ; OrderedLocusNames=ETEC_3241;
OS   Escherichia coli O78:H11 (strain H10407 / ETEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316401;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H10407 / ETEC;
RX   PubMed=20802035; DOI=10.1128/jb.00710-10;
RA   Crossman L.C., Chaudhuri R.R., Beatson S.A., Wells T.J., Desvaux M.,
RA   Cunningham A.F., Petty N.K., Mahon V., Brinkley C., Hobman J.L.,
RA   Savarino S.J., Turner S.M., Pallen M.J., Penn C.W., Parkhill J.,
RA   Turner A.K., Johnson T.J., Thomson N.R., Smith S.G., Henderson I.R.;
RT   "A commensal gone bad: complete genome sequence of the prototypical
RT   enterotoxigenic Escherichia coli strain H10407.";
RL   J. Bacteriol. 192:5822-5831(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1320-1519.
RC   STRAIN=H10407 / 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.
RN   [3]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=H10407 / ETEC;
RX   PubMed=22585966; DOI=10.1128/iai.06394-11;
RA   Strozen T.G., Li G., Howard S.P.;
RT   "YghG (GspSbeta) is a novel pilot protein required for localization of the
RT   GspSbeta type II secretion system secretin of enterotoxigenic Escherichia
RT   coli.";
RL   Infect. Immun. 80:2608-2622(2012).
CC   -!- FUNCTION: May be a substrate of the type II secretion system beta
CC       (T2SS-beta). {ECO:0000305|Ref.2}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC   -!- DISRUPTION PHENOTYPE: No effect on assembly or function of T2SS-beta.
CC       {ECO:0000269|PubMed:22585966}.
CC   -!- MISCELLANEOUS: Encoded in a type II secretion system (T2SS-beta); this
CC       strain encodes 2 T2SS but only this one (beta) is expressed under
CC       standard laboratory conditions. {ECO:0000305|PubMed:22585966}.
CC   -!- SIMILARITY: To V.cholerae AcfD (VC_0845). {ECO:0000305}.
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DR   EMBL; FN649414; CBJ02741.1; -; Genomic_DNA.
DR   EMBL; AY056599; AAL10688.1; -; Genomic_DNA.
DR   RefSeq; WP_001034464.1; NC_017633.1.
DR   AlphaFoldDB; E3PJ90; -.
DR   MEROPS; M98.001; -.
DR   EnsemblBacteria; CBJ02741; CBJ02741; ETEC_3241.
DR   KEGG; elh:ETEC_3241; -.
DR   HOGENOM; CLU_006312_0_0_6; -.
DR   OMA; VMGNARY; -.
DR   PHI-base; PHI:7003; -.
DR   Proteomes; UP000006877; 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 membrane; Lipoprotein; Membrane; Palmitate; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           24..1519
FT                   /note="Putative lipoprotein YghJ"
FT                   /id="PRO_0000405305"
FT   DOMAIN          1080..1380
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          1497..1519
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        1505..1519
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"
SQ   SEQUENCE   1519 AA;  168014 MW;  402DB4A166EE2165 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 WGEAISFGID TFELGSVRGN KSTIALTELG DEVRGANIDQ LIHRYSTTGQ
     NNTRVVPDDV RKVFAEYPNV INEIINLSLS NGATLGEGEQ VVNLPNEFIE QFNTGQAKEI
     DTAICAKTDG CNEARWFSLT TRNVNDGQIQ GVINKLWGVD TNYKSVSKFH VFHDSTNFYG
     STGNARGQAV VNISNAAFPI LMARNDKNYW LAFGEKRAWD KNELAYITEA PSIVRPENVT
     RETASFNLPF ISLGQVGDGK LMVIGNPHYN SILRCPNGYS WNGGVNKDGQ CTLNSDPDDM
     KNFMENVLRY LSNDRWLPDA KSSMTVGTNL ETVYFKKHGQ VLGNSAPFAF HKDFTGITVK
     PMTSYGNLNP DEVPLLILNG FEYVTQWGSD PYSIPLRADT SKPKLTQQDV TDLIAYMNKG
     GSVLIMENVM SNLKEESASG FVRLLDAAGL SMALNKSVVN NDPQGYPDRV RQRRSTPIWV
     YERYPAVDGK PPYTIDDTTK EVIWKYQQEN KPDDKPKLEV ASWQEEVEGK QVTQFAFIDE
     ADHKTPESLA AAKQRILDAF PGLEVCKDSD YHYEVNCLEY RPGTDVPVTG GMYVPQYTQL
     DLSADTAKAM LQAADLGTNI QRLYQHELYF RTNGRQGERL NSVDLERLYQ NMSVWLWNET
     KYRYEEGKED ELGFKTFTEF LNCYTNNAYV GTQCSAELKK SLIDNKMIYG EESSKAGMMN
     PSYPLNYMEK PLTRLMLGRS WWDLNIKVDV EKYPGVVNTN GETVTQNINL YSAPTKWFAG
     NMQSTGLWAP AQQEVSIESK STVPVTVTVA LADDLTGREK HEVSLNRPPR VTKTYDLKAN
     DKVTFKVPYG GLIYIKGDSK EVQSADFTFT GVVKAPFYKD GKWQHDLNSP APLGELESAS
     FVYTTPKKNL NASNYTGGLE QFANDLDTFA SSMNDFYGRD SEDGKHRMFT YKNLPGHKHR
     FANDVQISIG DAHSGYPVMN SSFSPNSTTL PTTPLNDWLI WHEVGHNAAE TPLTVPGATE
     VANNVLALYM QDRYLGKMNR VADDITVAPE YLEESNGQAW ARGGAGDRLL MYAQLKEWAE
     KNFDIKKWYP DGTPLPEFYS EREGMKGWNL FQLMHRKARG DEVSNDKFGG KNYCAESNGN
     AADTLMLCAS WVAQTDLSEF FKKWNPGANA YQLPGASEMS FEGGVSQSAY NTLASLDLPK
     PEQGPETINQ VTEHKMSAE