ID Q74C91_GEOSL Unreviewed; 574 AA.
AC Q74C91;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE SubName: Full=Type II secretion system ATPase PulE {ECO:0000313|EMBL:AAR35160.1};
GN Name=pulE {ECO:0000313|EMBL:AAR35160.1};
GN OrderedLocusNames=GSU1783 {ECO:0000313|EMBL:AAR35160.1};
OS Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=243231 {ECO:0000313|EMBL:AAR35160.1, ECO:0000313|Proteomes:UP000000577};
RN [1] {ECO:0000313|EMBL:AAR35160.1, ECO:0000313|Proteomes:UP000000577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51573 / DSM 12127 / PCA
RC {ECO:0000313|Proteomes:UP000000577};
RX PubMed=14671304; DOI=10.1126/science.1088727;
RA Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.,
RA Heidelberg J.F., Wu D., Wu M., Ward N., Beanan M.J., Dodson R.J.,
RA Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn M.,
RA Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J., Davidsen T.M.,
RA Zafar N., White O., Tran B., Romero C., Forberger H.A., Weidman J.,
RA Khouri H., Feldblyum T.V., Utterback T.R., Van Aken S.E., Lovley D.R.,
RA Fraser C.M.;
RT "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT environments.";
RL Science 302:1967-1969(2003).
CC -!- SIMILARITY: Belongs to the GSP E family.
CC {ECO:0000256|ARBA:ARBA00006611}.
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DR EMBL; AE017180; AAR35160.1; -; Genomic_DNA.
DR RefSeq; NP_952833.1; NC_002939.5.
DR RefSeq; WP_010942427.1; NC_002939.5.
DR AlphaFoldDB; Q74C91; -.
DR SMR; Q74C91; -.
DR STRING; 243231.GSU1783; -.
DR EnsemblBacteria; AAR35160; AAR35160; GSU1783.
DR KEGG; gsu:GSU1783; -.
DR PATRIC; fig|243231.5.peg.1822; -.
DR eggNOG; COG2804; Bacteria.
DR HOGENOM; CLU_013446_10_1_7; -.
DR InParanoid; Q74C91; -.
DR OrthoDB; 9805147at2; -.
DR Proteomes; UP000000577; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
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 Gene3D; 3.30.300.160; Type II secretion system, protein E, N-terminal domain; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001482; T2SS/T4SS_dom.
DR InterPro; IPR037257; T2SS_E_N_sf.
DR InterPro; IPR007831; T2SS_GspE_N.
DR PANTHER; PTHR30258:SF2; BACTERIOPHAGE ADSORPTION PROTEIN B; 1.
DR PANTHER; PTHR30258; TYPE II SECRETION SYSTEM PROTEIN GSPE-RELATED; 1.
DR Pfam; PF05157; MshEN; 1.
DR Pfam; PF00437; T2SSE; 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 Reference proteome {ECO:0000313|Proteomes:UP000000577}.
FT DOMAIN 391..405
FT /note="Bacterial type II secretion system protein E"
FT /evidence="ECO:0000259|PROSITE:PS00662"
SQ SEQUENCE 574 AA; 64239 MW; D65B43C409B2EBF6 CRC64;
MEKQSFKRKT IGQILVQQGS LNPDQIPYLV EKRNASTKRF GEVCVGDGLI TEENLARALA
EQFGLDYVDA RGVRLNESLL ATLPPDAIYR YQFVPLEEED GTLVVLIADP TDVLKLDELE
LLLDRPFIVK LATETAIATI LKKGEATSRV LKEVSEDFML QLVKENEKGE EILSMEKISA
DTSPIIKLVN STVMDALTRR ASDIHIETAL EGVIIKYRID GVLYRATEPL DIHFQAPIIS
RLKVMSELDI SERRIPQDGR FKVRLNDKAI DFRVSIMPSA FGEDAVIRIL DKESIASDLK
GLTLETLGMH PREMKRLRRK IREPYGMVLV TGPTGSGKTT TLYAALTEIH TGEEKIITIE
DPVEYVLRGI VQIPVNEKKG LTFARGLRSI LRHDPDKIMV GEIRDPETAQ IAVQSALTGH
LVFTTVHANN AFDVLGRFIH MGIDPYNFVS CLNCVMAQRL VRKACPHCKY PVEHSDSVLI
ESGLDPEECR DVTFYESRGC EECNGTGYRG RSAIIELLDL NDQMRELIMA KAPAAQLKAA
ARESGTVFLR ESAIEKVFAG ETTLREINRV TFVE
//
