ID A0A0Q8XJT4_9SPHN Unreviewed; 441 AA.
AC A0A0Q8XJT4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Type III secretion apparatus H+-transporting two-sector ATPase {ECO:0000313|EMBL:KRC81380.1};
GN Name=fliI {ECO:0000313|EMBL:KRC81380.1};
GN ORFNames=ASE13_03015 {ECO:0000313|EMBL:KRC81380.1};
OS Sphingomonas sp. Root241.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736501 {ECO:0000313|EMBL:KRC81380.1, ECO:0000313|Proteomes:UP000051629};
RN [1] {ECO:0000313|EMBL:KRC81380.1, ECO:0000313|Proteomes:UP000051629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root241 {ECO:0000313|EMBL:KRC81380.1,
RC ECO:0000313|Proteomes:UP000051629};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRC81380.1, ECO:0000313|Proteomes:UP000051629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root241 {ECO:0000313|EMBL:KRC81380.1,
RC ECO:0000313|Proteomes:UP000051629};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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 -!- 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:KRC81380.1}.
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DR EMBL; LMIV01000001; KRC81380.1; -; Genomic_DNA.
DR RefSeq; WP_056611241.1; NZ_LMIV01000001.1.
DR AlphaFoldDB; A0A0Q8XJT4; -.
DR STRING; 1736501.ASE13_03015; -.
DR OrthoDB; 9803053at2; -.
DR Proteomes; UP000051629; 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; IPR020003; ATPase_a/bsu_AS.
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.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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}.
FT DOMAIN 163..344
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 441 AA; 46928 MW; D135D7223E7CF88B CRC64;
MADGPLATVD QLLAGLQRSP TVERRGRLVE VLGTTLKVTG IAPRVGDFCE VIEPSTGRVV
PVEVVGIAGQ ATILTPLGDV RGLSVDAEVI VRSGADLVPW GEELLGRVLD GRGRPIDGRG
ELPADLKRRP LHAPAPQPME RALIDAPLPT GVRAIDTLLT LGRGQRLGVF AAAGGGKSTL
LGMLARFAEA DVIVIALIGE RGREVREFIE DALGEAGLAR SVIVCATSDR AAMERVRAAH
HATAVAEGFR SEGRSVLLLM DSVTRFARAL REIGLAAGEP PVRRGFPPSV FAELPRLFER
AGNDATGSIT GIYTVLLEDE EGDDPIGEEV RSILDGHVIL SRKLGAAGHY PAIDVLASLS
RLFPRLATPA HREAATRVRA LLAKHAEIEF LVQVGEYRAG ADPLADRAIA ARPEIDTLLR
QDTDRPEDFQ TSLMLLRGVA G
//
