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Database: UniProt
Entry: D3SGV3_THISK
LinkDB: D3SGV3_THISK
Original site: D3SGV3_THISK 
ID   D3SGV3_THISK            Unreviewed;       491 AA.
AC   D3SGV3;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   24-JAN-2024, entry version 71.
DE   SubName: Full=Type II secretion system protein E {ECO:0000313|EMBL:ADC73344.1};
GN   ORFNames=TK90_2860 {ECO:0000313|EMBL:ADC73344.1};
OS   Thioalkalivibrio sp. (strain K90mix).
OG   Plasmid pTK9001 {ECO:0000313|EMBL:ADC73344.1,
OG   ECO:0000313|Proteomes:UP000009099}.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thioalkalivibrio.
OX   NCBI_TaxID=396595 {ECO:0000313|EMBL:ADC73344.1, ECO:0000313|Proteomes:UP000009099};
RN   [1] {ECO:0000313|EMBL:ADC73344.1, ECO:0000313|Proteomes:UP000009099}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K90mix {ECO:0000313|EMBL:ADC73344.1,
RC   ECO:0000313|Proteomes:UP000009099};
RC   PLASMID=pTK9001 {ECO:0000313|EMBL:ADC73344.1,
RC   ECO:0000313|Proteomes:UP000009099};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Foster B., Sun H., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Sorokin D.Y., Muyzer G., Woyke T.;
RT   "Complete sequence of plasmid of Thioalkalivibrio sp. K90mix.";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GSP E family.
CC       {ECO:0000256|ARBA:ARBA00006611}.
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DR   EMBL; CP001906; ADC73344.1; -; Genomic_DNA.
DR   RefSeq; WP_013006709.1; NC_013930.1.
DR   AlphaFoldDB; D3SGV3; -.
DR   KEGG; tkm:TK90_2860; -.
DR   eggNOG; COG2804; Bacteria.
DR   HOGENOM; CLU_013446_10_6_6; -.
DR   OrthoDB; 9776961at2; -.
DR   Proteomes; UP000009099; Plasmid pTK9001.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd01129; PulE-GspE-like; 1.
DR   Gene3D; 3.30.450.90; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001482; T2SS/T4SS_dom.
DR   InterPro; IPR037257; T2SS_E_N_sf.
DR   PANTHER; PTHR30258:SF2; BACTERIOPHAGE ADSORPTION PROTEIN B; 1.
DR   PANTHER; PTHR30258; TYPE II SECRETION SYSTEM PROTEIN GSPE-RELATED; 1.
DR   Pfam; PF00437; T2SSE; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF160246; EspE N-terminal domain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00662; T2SP_E; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Plasmid {ECO:0000313|EMBL:ADC73344.1}.
FT   DOMAIN          344..358
FT                   /note="Bacterial type II secretion system protein E"
FT                   /evidence="ECO:0000259|PROSITE:PS00662"
SQ   SEQUENCE   491 AA;  54451 MW;  884F7BC3A719E624 CRC64;
     MQILNRTDGS TQRLGELLIE RGLLSSGALD ASLTEQRLTG ERLGRIMVRN GFVTRKQLLA
     TLADTENPEV LSEPFESDRV PPEVLLELRT MLLGDTGDRL LLASDAPRWW VERVLGPYFP
     GHRMIWMDFD PEIHARHLEL LAAYTSETVL DRLLRRAVME GISDIHLIPK PAAYTVMYRR
     LGVRQIIEDR TREEGIRMVA QAKDRAKVDI AETSVPQDGA FRLAMLDRSV DFRVATIPET
     DGEKLVIRVL DPEAAYPELE ALGMREVDTW MDAAAQPHGI CLICGATGSG KSTTLNATLR
     RLDRFGMSIQ TVEDPVEHQL SFVGQVEVNR GRGLDFTRAL RGFMRADPDV LIVGEIRDRE
     TAELAVQAAE TGHMVFATLH TDSAAGGLTR LRDLGVPIAD FAPLVRATMA QKLIRVACPH
     CHGKGCDACE GIGYSGRTLI SEVAPFRGPQ DVERALNGET WWTSLREDGE ARLREGSTTD
     DEIRRVLGSG L
//
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