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Database: UniProt
Entry: C6HWN2_9BACT
LinkDB: C6HWN2_9BACT
Original site: C6HWN2_9BACT 
ID   C6HWN2_9BACT            Unreviewed;       457 AA.
AC   C6HWN2;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Flagellar protein export ATPase FliI {ECO:0000313|EMBL:EES53008.1};
GN   ORFNames=UBAL3_80630065 {ECO:0000313|EMBL:EES53008.1};
OS   Leptospirillum ferrodiazotrophum.
OC   Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC   Leptospirillum.
OX   NCBI_TaxID=412449 {ECO:0000313|EMBL:EES53008.1, ECO:0000313|Proteomes:UP000009374};
RN   [1] {ECO:0000313|EMBL:EES53008.1, ECO:0000313|Proteomes:UP000009374}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=19429552; DOI=10.1128/AEM.02943-08;
RA   Goltsman D.S., Denef V.J., Singer S.W., VerBerkmoes N.C., Lefsrud M.,
RA   Mueller R.S., Dick G.J., Sun C.L., Wheeler K.E., Zemla A., Baker B.J.,
RA   Hauser L., Land M., Shah M.B., Thelen M.P., Hettich R.L., Banfield J.F.;
RT   "Community genomic and proteomic analyses of chemoautotrophic iron-
RT   oxidizing "Leptospirillum rubarum" (Group II) and "Leptospirillum
RT   ferrodiazotrophum" (Group III) bacteria in acid mine drainage biofilms.";
RL   Appl. Environ. Microbiol. 75:4599-4615(2009).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   EMBL; GG693870; EES53008.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6HWN2; -.
DR   Proteomes; UP000009374; 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: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; 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; 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   Cell projection {ECO:0000313|EMBL:EES53008.1};
KW   Cilium {ECO:0000313|EMBL:EES53008.1};
KW   Flagellum {ECO:0000313|EMBL:EES53008.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009374};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          169..352
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   457 AA;  49678 MW;  78837B848008F580 CRC64;
     MITIGRDVAT DHRWLDGVGE KMEALLSDFS PDQEGGLVVQ GVGLMIEAKG MSLGVGEICT
     LLSDPPVDAE VVGFREGRTL LMPLGDLEGV RPGTRLVRKS RITSVRISPH WLGRVLDPLG
     RPMDGRPLPP GTVEVPLRGR PLNPLLRRRI ERPLDLSVRS INALATVGEG QKIGIFAGPG
     VGKSTLMGMM ARNASVDVNV IALIGERGRE VREFLERDLG PEGLSRTVLV VATGELPPLL
     KTRATHFAMA IAEMFRDRGQ NVLFMMDSLT RYAGALREIG LATGEPPSAR GFTPSVFAQL
     PRLVERAGCA EGPGSITGIY TVLVEGEDLP DDPLSEALTA ILDGHIHLSR TLAHEGVFPA
     VEPMGSLSRV MADIVDEDRQ VLAREWRRLY GLYRRSEDLI RIGAYVAGGD PELDRAVRLH
     ESMTGFLRQG REERVGLEEA FEDLARSLDE REGGSDG
//
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