ID Q893Y3_CLOTE Unreviewed; 446 AA.
AC Q893Y3;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 129.
DE SubName: Full=Flagellum-specific ATP synthase {ECO:0000313|EMBL:AAO36209.1};
DE EC=3.6.3.14 {ECO:0000313|EMBL:AAO36209.1};
GN OrderedLocusNames=CTC_01673 {ECO:0000313|EMBL:AAO36209.1};
OS Clostridium tetani (strain Massachusetts / E88).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=212717 {ECO:0000313|EMBL:AAO36209.1, ECO:0000313|Proteomes:UP000001412};
RN [1] {ECO:0000313|EMBL:AAO36209.1, ECO:0000313|Proteomes:UP000001412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Massachusetts / E88 {ECO:0000313|Proteomes:UP000001412};
RX PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA Brueggemann H., Baumer S., Fricke W.F., Wiezer A., Liesegang H., Decker I.,
RA Herzberg C., Martinez-Arias R., Merkl R., Henne A., Gottschalk G.;
RT "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; AE015927; AAO36209.1; -; Genomic_DNA.
DR AlphaFoldDB; Q893Y3; -.
DR STRING; 212717.CTC_01673; -.
DR KEGG; ctc:CTC_01673; -.
DR HOGENOM; CLU_022398_5_1_9; -.
DR Proteomes; UP000001412; Chromosome.
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; 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; 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; 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 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.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000313|EMBL:AAO36209.1};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000001412};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 163..344
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 446 AA; 48991 MW; 8D79C92E8E0EB29F CRC64;
MDWSVSMELL DFNYINKKIK ETDYYSYEGV VKKVIGLTIE VEGIKAFIGE VCTIYNQQNN
PIVCEVVGFV EDNVILMPLG ELIGIAPGCR VIPSGNPLSV KCSEELFGKV LDGLGSPLNG
EKIKTGVPYP LDREPPDPLK RRRIKDVIPT GVRAIDGYLT CGEGQRIGIF AGSGVGKSTS
LGMIAKYAEA DVNVICLIGE RGREVLDFVE KDLGEEGMKK SIVICATSDK PALVRIKGAF
TATAIAEYFR DKGKKVILMM DSVTRFAMAQ REVGLAIGEP PATKGYTPSV FAMLPRLMER
SGMSDKGSIT AFYTVLVDGD DFNEPIADAV RGILDGHIVL SRDLAAKNHY PAIDILSSIS
RLMNEISVKE HKESASIGRD LIATYKEAED LINIGAYVKG SNEKIDIAIK YIDSINEFLT
QKVDEHNNFE ESIQWLNSIF KNLRSN
//
