ID Q2II92_ANADE Unreviewed; 435 AA.
AC Q2II92;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE SubName: Full=Type III secretion system ATPase, FliI/YscN {ECO:0000313|EMBL:ABC81369.1};
DE EC=3.6.3.15 {ECO:0000313|EMBL:ABC81369.1};
GN OrderedLocusNames=Adeh_1596 {ECO:0000313|EMBL:ABC81369.1};
OS Anaeromyxobacter dehalogenans (strain 2CP-C).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Anaeromyxobacteraceae; Anaeromyxobacter.
OX NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC81369.1, ECO:0000313|Proteomes:UP000001935};
RN [1] {ECO:0000313|Proteomes:UP000001935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R.,
RA Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N.,
RA Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R.,
RA Zhulin I.B., Loeffler F.E., Richardson P.;
RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL Submitted (JAN-2006) 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}.
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DR EMBL; CP000251; ABC81369.1; -; Genomic_DNA.
DR RefSeq; WP_011420652.1; NC_007760.1.
DR AlphaFoldDB; Q2II92; -.
DR STRING; 290397.Adeh_1596; -.
DR KEGG; ade:Adeh_1596; -.
DR eggNOG; COG1157; Bacteria.
DR HOGENOM; CLU_022398_5_1_7; -.
DR OrthoDB; 9801639at2; -.
DR Proteomes; UP000001935; 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:0030254; P:protein secretion by the type III secretion system; IEA:InterPro.
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; IPR027417; P-loop_NTPase.
DR InterPro; IPR040627; T3SS_ATPase_C.
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.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000313|EMBL:ABC81369.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000001935};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 157..338
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 435 AA; 45018 MW; D3CDF1D83DF6487A CRC64;
MTVDLGRVRT ALGEAAPLPL RGRVTRLTGL VLEAAVGGVR QGEAVELRAP GREPLLAEVV
GLRDDRAVLV PFGELGGVGL DAEVIPTGRP HAIRVGPGLL GRVLDGLGRP LDGAPLPAGL
EEWAVDRPAP NPLARRPVAA PLPLGVRVLD GLLTAGEGQR IGLFAGSGVG KSTLLGQLAR
GARADLCVVC LVGERGREVR EFLEGPLGAD GLARSVVVAA TSDAPALVRL KAAHVATAVA
EWFAERGDRV LLLVDSVTRY ARALREVGLA AGEPPARQGY PPSVFAALPR LLERAGNRAR
GGITAVYTVL VAGGDLEEPI ADEVRGILDG HVVLDRAVAA GGRFPAVDPL QSLSRVMPAV
AGPDHLAAAG RVRALLAAHA RVRDLVALGA YRAGGDPEAD LALARLPALE AFLRQPLGEP
APFEETLRRL EALAG
//
