ID Q87GH8_VIBPA Unreviewed; 420 AA.
AC Q87GH8;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE RecName: Full=protein-secreting ATPase {ECO:0000256|ARBA:ARBA00024382};
DE EC=7.4.2.8 {ECO:0000256|ARBA:ARBA00024382};
GN OrderedLocusNames=VPA1338 {ECO:0000313|EMBL:BAC62681.1};
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926 {ECO:0000313|EMBL:BAC62681.1, ECO:0000313|Proteomes:UP000002493};
RN [1] {ECO:0000313|EMBL:BAC62681.1, ECO:0000313|Proteomes:UP000002493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633 {ECO:0000313|Proteomes:UP000002493};
RX PubMed=12620739; DOI=10.1016/S0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; BA000032; BAC62681.1; -; Genomic_DNA.
DR RefSeq; NP_800848.1; NC_004605.1.
DR RefSeq; WP_005463220.1; NC_004605.1.
DR AlphaFoldDB; Q87GH8; -.
DR GeneID; 1192034; -.
DR KEGG; vpa:VPA1338; -.
DR PATRIC; fig|223926.6.peg.4261; -.
DR eggNOG; COG1157; Bacteria.
DR HOGENOM; CLU_022398_5_1_6; -.
DR Proteomes; UP000002493; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd01136; ATPase_flagellum-secretory_path_III; 1.
DR Gene3D; 1.20.1270.330; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR040627; T3SS_ATPase_C.
DR NCBIfam; NF040574; T3SS_ATP_VscN2; 1.
DR PANTHER; PTHR15184; ATP SYNTHASE; 1.
DR PANTHER; PTHR15184:SF9; SPI-1 TYPE 3 SECRETION SYSTEM ATPASE; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF18269; T3SS_ATPase_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002493};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 145..323
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 420 AA; 46941 MW; F9B12D30708D7896 CRC64;
MLKYFFKVKE SYQDTVICHV NIDTFVGQEC FVHTITGERI RGEIVKVTGS KLEIKLLQPG
SVQRGGKVEI TPRRFCFPLN ESALVGKVIN CYGETLYGDS YLGQPGEFID LPIAVEPIPL
QMRAPIETVF PTKLKIIDGL FTIGEGQRLG LFAPAGAGKT TTVSIMANNM DADVVIFAMI
GERAREVVEF LEGEIGPEVI RKSITIVSTS EANPLEKVRS GLVAVSIARY YMEQGKKVVL
YFDSLTRFAR AQAMLDGTPI KGGIPIGVSL ALSRLVESCG NSIQGSVTGI FTVLIEKEID
DDPIAHEVKS LIDGHLVYST TIAATGRYPA IDVLKSKSRL QNKVQEKYYV RLSEKIKDMV
YRYFNVELLI RVGEYEKGND LETDEAIERY PKIIEFLKQG FEGVEYEETL QEMERIWSNY
//
