ID C4K6D2_HAMD5 Unreviewed; 431 AA.
AC C4K6D2;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=protein-secreting ATPase {ECO:0000256|ARBA:ARBA00024382};
DE EC=7.4.2.8 {ECO:0000256|ARBA:ARBA00024382};
GN Name=invC {ECO:0000313|EMBL:ACQ68125.1};
GN OrderedLocusNames=HDEF_1501 {ECO:0000313|EMBL:ACQ68125.1};
OS Hamiltonella defensa subsp. Acyrthosiphon pisum (strain 5AT).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; aphid secondary symbionts; Hamiltonella.
OX NCBI_TaxID=572265 {ECO:0000313|EMBL:ACQ68125.1, ECO:0000313|Proteomes:UP000002334};
RN [1] {ECO:0000313|EMBL:ACQ68125.1, ECO:0000313|Proteomes:UP000002334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5AT {ECO:0000313|Proteomes:UP000002334};
RX PubMed=19451630; DOI=10.1073/pnas.0900194106;
RA Degnan P.H., Yu Y., Sisneros N., Wing R.A., Moran N.A.;
RT "Hamiltonella defensa, genome evolution of protective bacterial
RT endosymbiont from pathogenic ancestors.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:9063-9068(2009).
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; CP001277; ACQ68125.1; -; Genomic_DNA.
DR RefSeq; WP_015873893.1; NC_012751.1.
DR AlphaFoldDB; C4K6D2; -.
DR STRING; 572265.HDEF_1501; -.
DR GeneID; 66261150; -.
DR KEGG; hde:HDEF_1501; -.
DR eggNOG; COG1157; Bacteria.
DR HOGENOM; CLU_022398_5_1_6; -.
DR Proteomes; UP000002334; 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; cd01426; ATP-synt_F1_V1_A1_AB_FliI_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; 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 153..334
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 431 AA; 47482 MW; 007F7A23ACECB819 CRC64;
MHKLRLLRYK AHPLRLSGPI IEARLFGVKI GEICDIRSDC SESEVICRAQ VLGFYNDRSV
LSLIGNARGL SRDVVIIPTG AALLVTIDDS LLGSVVDPSG KIVAHLSEPT EIMHNPSIRA
IDSPPPSYLH RLSIRDPFIT GVKAIDGLIT CGVGQRMGIF AAAGCGKTSL MHMLIEQADA
DVFVIGLVGE RGREVTEFTE VLSKSGRAQK CIVVYATSDF SSLDRCNAAL LATTIAEYFR
DQGKKVVLFL DSITRYARAL RDVALAAGEA PARRGYPASV FDSLPSILER PSNTKNGSIT
AFYTILLESD DEPDPISEEI RSILDGHIYL SKKLAIKNHY PAIDVLHSIS RVSSQICDTN
HLSMAGEFRN ILAKIQELQM FVELGEYRQG ENAENDRAIK KRPALLKWLQ QSMNEHSSFE
QTLQAMNELT Q
//
