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Database: UniProt
Entry: E3D9G8_GARV3
LinkDB: E3D9G8_GARV3
Original site: E3D9G8_GARV3 
ID   E3D9G8_GARV3            Unreviewed;       282 AA.
AC   E3D9G8;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Lipoprotein {ECO:0000256|PIRNR:PIRNR002854};
GN   OrderedLocusNames=HMPREF0421_20630 {ECO:0000313|EMBL:ADP38712.1};
OS   Gardnerella vaginalis (strain ATCC 14019 / 317).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Gardnerella.
OX   NCBI_TaxID=525284 {ECO:0000313|EMBL:ADP38712.1, ECO:0000313|Proteomes:UP000001453};
RN   [1] {ECO:0000313|EMBL:ADP38712.1, ECO:0000313|Proteomes:UP000001453}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14019 / 317 {ECO:0000313|Proteomes:UP000001453};
RX   PubMed=20865041; DOI=10.1371/journal.pone.0012411;
RA   Yeoman C.J., Yildirim S., Thomas S.M., Durkin A.S., Torralba M., Sutton G.,
RA   Buhay C.J., Ding Y., Dugan-Rocha S.P., Muzny D.M., Qin X., Gibbs R.A.,
RA   Leigh S.R., Stumpf R., White B.A., Highlander S.K., Nelson K.E.,
RA   Wilson B.A.;
RT   "Comparative genomics of Gardnerella vaginalis strains reveals substantial
RT   differences in metabolic and virulence potential.";
RL   PLoS ONE 5:E12411-E12411(2010).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-
CC       anchor {ECO:0000256|ARBA:ARBA00004635}.
CC   -!- SIMILARITY: Belongs to the nlpA lipoprotein family.
CC       {ECO:0000256|PIRNR:PIRNR002854}.
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DR   EMBL; CP002104; ADP38712.1; -; Genomic_DNA.
DR   RefSeq; WP_004112601.1; NC_014644.1.
DR   RefSeq; YP_003985735.1; NC_014644.1.
DR   AlphaFoldDB; E3D9G8; -.
DR   GeneID; 60756190; -.
DR   KEGG; gvg:HMPREF0421_20630; -.
DR   PATRIC; fig|525284.18.peg.627; -.
DR   HOGENOM; CLU_067080_0_0_11; -.
DR   OrthoDB; 9812878at2; -.
DR   Proteomes; UP000001453; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   InterPro; IPR004872; Lipoprotein_NlpA.
DR   PANTHER; PTHR30429; D-METHIONINE-BINDING LIPOPROTEIN METQ; 1.
DR   PANTHER; PTHR30429:SF0; METHIONINE-BINDING LIPOPROTEIN METQ; 1.
DR   Pfam; PF03180; Lipoprotein_9; 1.
DR   PIRSF; PIRSF002854; MetQ; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Lipoprotein {ECO:0000256|PIRNR:PIRNR002854, ECO:0000313|EMBL:ADP38712.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           35..282
FT                   /note="Lipoprotein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003168152"
FT   LIPID           28
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002854-1"
SQ   SEQUENCE   282 AA;  30358 MW;  BC5954F86D20AA37 CRC64;
     MKITKKNTKI IAAFTALTAI LGLSLSACGS SANGATKDDK VIKVAASPTP HSDILNKVVK
     PILQKQGYKL VVKEFTDYVQ PNTAVEEGEA DANYHQHLPY LDNFNKERGT HIISIAGIHF
     EPFGLYPGKT KTIKDLKDGA TVAVPSDPTN EARALLLLQD AGLLKLKNPK DVNATKKDIV
     SNPKNLKFKE IDAALVPTVV KDVDLAALNG NYAIQAGFNP TKDPLTSEKV GGVAAKTYEN
     IIAVKKGSEK LAKIKALVKA LKTDAVRDFI KKNYNGAVLP VF
//
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