ID A0A2S8WVC9_9MICC Unreviewed; 439 AA.
AC A0A2S8WVC9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=EscN/YscN/HrcN family type III secretion system ATPase {ECO:0000313|EMBL:PQZ96040.1};
GN ORFNames=CQ018_01785 {ECO:0000313|EMBL:PQZ96040.1};
OS Arthrobacter sp. MYb227.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1848601 {ECO:0000313|EMBL:PQZ96040.1, ECO:0000313|Proteomes:UP000239972};
RN [1] {ECO:0000313|EMBL:PQZ96040.1, ECO:0000313|Proteomes:UP000239972}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MYb227 {ECO:0000313|EMBL:PQZ96040.1,
RC ECO:0000313|Proteomes:UP000239972};
RA Zimmermann J., Obeng N., Yang W., Obeng O., Kissoyan K., Pees B.,
RA Dirksen P., Hoppner M., Franke A., Rosenstiel P., Leippe M., Dierking K.,
RA Kaleta C., Schulenburg H.;
RT "Genomic, metabolic, and phenotypic characteristics of bacterial isolates
RT from the natural microbiome of the model nematode Caenorhabditis elegans.";
RL Submitted (SEP-2017) 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:PQZ96040.1}.
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DR EMBL; PCPT01000001; PQZ96040.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S8WVC9; -.
DR OrthoDB; 9801639at2; -.
DR Proteomes; UP000239972; 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 Reference proteome {ECO:0000313|Proteomes:UP000239972};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 156..337
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 439 AA; 46291 MW; E0B25F513BCA4C18 CRC64;
MRSNTLAWPE LELALTAAAP ARLGVVTSVV GLGLEISGLN APLGTVLEIG EQKVSAEVVA
ARRSTLHCMP LGEIEKISVG DLVFNSGSAA SVPTGPGLLG RVLDGLGNPI DGKGPLGEQQ
LVPMEHTTPA ALERTRITES LHLGVRVMDT LTAVGAGQRI GLFAGSGVGK SSLLSMIARG
SAAQINVIAL VGERGREVRE FLEEDLGPEG LARSIVVVST ADEPARMRLR AAFVATRIAE
SFRESGAQVL LMMDSLTRVA MAQREIGLSA GEPPATRGYP PSTFSLLARL LERAGSDAHG
SITGIYTVLV DGDDHNEPIA DSTRSLLDGH IVLDRKLAVA GHFPSIDALA SVSRVANRVT
TREQAKAAAT LRRVMAARRS VQDLLDVGAY QRGSNPLVDT AVDNEQAINN FLRQRLEEPV
PGEQAWSELA NLLQTLGVN
//
