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Database: UniProt
Entry: D4S578_9FIRM
LinkDB: D4S578_9FIRM
Original site: D4S578_9FIRM 
ID   D4S578_9FIRM            Unreviewed;       461 AA.
AC   D4S578;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=Type 3 secretion system ATPase {ECO:0000256|ARBA:ARBA00024442};
DE            EC=7.4.2.8 {ECO:0000256|ARBA:ARBA00024382};
GN   Name=fliI {ECO:0000313|EMBL:EFF66498.1};
GN   ORFNames=HMPREF7545_0693 {ECO:0000313|EMBL:EFF66498.1};
OS   Selenomonas noxia ATCC 43541.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC   Selenomonas.
OX   NCBI_TaxID=585503 {ECO:0000313|EMBL:EFF66498.1, ECO:0000313|Proteomes:UP000003701};
RN   [1] {ECO:0000313|EMBL:EFF66498.1, ECO:0000313|Proteomes:UP000003701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43541 {ECO:0000313|EMBL:EFF66498.1,
RC   ECO:0000313|Proteomes:UP000003701};
RA   Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA   Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA   Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA   Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA   Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA   Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA   Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA   Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA   Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA   Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL   Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + cellular proteinSide 1 = ADP + phosphate +
CC         cellular proteinSide 2.; EC=7.4.2.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00034006};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. T3SS ATPase
CC       subfamily. {ECO:0000256|ARBA:ARBA00024342}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFF66498.1}.
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DR   EMBL; ACKT01000016; EFF66498.1; -; Genomic_DNA.
DR   RefSeq; WP_006694583.1; NZ_GG749280.1.
DR   AlphaFoldDB; D4S578; -.
DR   GeneID; 84786388; -.
DR   eggNOG; COG1157; Bacteria.
DR   HOGENOM; CLU_022398_5_1_9; -.
DR   InParanoid; D4S578; -.
DR   OrthoDB; 9803053at2; -.
DR   Proteomes; UP000003701; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030257; C:type III protein secretion system complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR   GO; GO:0044780; P:bacterial-type flagellum assembly; IEA:InterPro.
DR   GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:InterPro.
DR   GO; GO:0030254; P:protein secretion by the type III secretion system; IEA:InterPro.
DR   CDD; cd18114; ATP-synt_flagellum-secretory_path_III_C; 1.
DR   CDD; cd18117; ATP-synt_flagellum-secretory_path_III_N; 1.
DR   CDD; cd01136; ATPase_flagellum-secretory_path_III; 1.
DR   Gene3D; 3.40.50.12240; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR005714; ATPase_T3SS_FliI/YscN.
DR   InterPro; IPR013380; ATPase_T3SS_SctN.
DR   InterPro; IPR022425; FliI_clade2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR040627; T3SS_ATPase_C.
DR   NCBIfam; TIGR03497; FliI_clade2; 1.
DR   NCBIfam; TIGR01026; fliI_yscN; 1.
DR   NCBIfam; TIGR02546; III_secr_ATP; 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; PF02874; ATP-synt_ab_N; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell projection {ECO:0000313|EMBL:EFF66498.1};
KW   Cilium {ECO:0000313|EMBL:EFF66498.1};
KW   Flagellum {ECO:0000313|EMBL:EFF66498.1};
KW   Hydrolase {ECO:0000313|EMBL:EFF66498.1};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transport {ECO:0000256|ARBA:ARBA00022448};
KW   Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT   DOMAIN          170..352
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   461 AA;  49547 MW;  B1D3ED1F20C9D30F CRC64;
     MNMSETGGNP PFSIDIHKFQ DALRACSPMK LTGKVTQIIG LVIESQGPTV TVGELCYVSS
     HFSGMPPVPA EVVGFREGSV LLMPVGEMQG IGPGCEVIAT GRRLRVKVGE ELLGRVLDGL
     GNPIDGKGPI LAQEEYPLQA PPPPPLTRPR IHDNLYVGVR AIDGLITLGD GQRIGIMAGS
     GVGKSTLLSM IARNTEADIS VITLVGERGR EVRDFIERDL GEEGLKRSVV VVATSDQPAL
     VRIKGAMTGT AIAEYFRDQG HKVVLMMDSV TRFAMAQREV GLTIGEPPAT RGYTPSVFAM
     LPRLLERAGT SERGSITGIY TVLVDGDDMN EPIADAVRSI LDGHIVLSRR IAAQNHFPAI
     DVLGSVSRVM YEVVDKSHLE AAQEMRQLMA VYAEAEDLIH IGAYVKGSSP KIDAAIQKID
     GINEFLRQDI YEVTSYEETE QQLLAAVGKS EPAPAPAEES T
//
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