ID Q5KXT4_GEOKA Unreviewed; 492 AA.
AC Q5KXT4;
DT 01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 01-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Stage IV sporulation protein A {ECO:0000256|PIRNR:PIRNR007466};
DE EC=3.6.1.- {ECO:0000256|PIRNR:PIRNR007466};
DE AltName: Full=Coat morphogenetic protein SpoIVA {ECO:0000256|PIRNR:PIRNR007466};
GN Name=spoIVA {ECO:0000313|EMBL:BAD76502.1};
GN OrderedLocusNames=GK2217 {ECO:0000313|EMBL:BAD76502.1};
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909 {ECO:0000313|EMBL:BAD76502.1, ECO:0000313|Proteomes:UP000001172};
RN [1] {ECO:0000313|EMBL:BAD76502.1, ECO:0000313|Proteomes:UP000001172}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426 {ECO:0000313|EMBL:BAD76502.1,
RC ECO:0000313|Proteomes:UP000001172};
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(2004).
CC -!- FUNCTION: ATPase. Has a role at an early stage in the morphogenesis of
CC the spore coat. {ECO:0000256|PIRNR:PIRNR007466}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|PIRNR:PIRNR007466};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR007466}.
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DR EMBL; BA000043; BAD76502.1; -; Genomic_DNA.
DR RefSeq; WP_011231701.1; NC_006510.1.
DR AlphaFoldDB; Q5KXT4; -.
DR STRING; 235909.GK2217; -.
DR KEGG; gka:GK2217; -.
DR eggNOG; COG0699; Bacteria.
DR HOGENOM; CLU_043635_0_0_9; -.
DR Proteomes; UP000001172; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR CDD; cd00882; Ras_like_GTPase; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR046842; SpoIVA_ATPase.
DR InterPro; IPR046840; SpoIVA_C.
DR InterPro; IPR046841; SpoIVA_middle.
DR InterPro; IPR014201; Spore_IV_A.
DR NCBIfam; TIGR02836; spore_IV_A; 1.
DR Pfam; PF09547; SpoIVA_ATPase; 1.
DR Pfam; PF20439; SpoIVA_C; 1.
DR Pfam; PF20438; SpoIVA_middle; 1.
DR PIRSF; PIRSF007466; SpoIVA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR007466};
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR007466};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR007466};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR007466};
KW Reference proteome {ECO:0000313|Proteomes:UP000001172};
KW Sporulation {ECO:0000256|PIRNR:PIRNR007466}.
FT DOMAIN 1..237
FT /note="Stage IV sporulation protein A ATPase"
FT /evidence="ECO:0000259|Pfam:PF09547"
FT DOMAIN 239..416
FT /note="Stage IV sporulation protein A middle"
FT /evidence="ECO:0000259|Pfam:PF20438"
FT DOMAIN 417..492
FT /note="Sporulation stage IV protein A C-terminal"
FT /evidence="ECO:0000259|Pfam:PF20439"
SQ SEQUENCE 492 AA; 55427 MW; 3CE5768B620CD0D7 CRC64;
MEKVDIFKDI AERTGGDIYL GVVGAVRTGK STFIKRFMEL VVIPNIKNEA DKARAQDELP
QSAAGKTIMT TEPKFVPNQA VTVKVDEGLE VNIRLVDCVG YAVPGAKGYE DENGPRMIHT
PWYEEPIPFQ EAAEIGTRKV IQEHSTIGVV ITTDGTIGEI PRQDYVEAEE RVISELKEVG
KPFIMIVNTV RPHHPETEAL RRELAEKYDI PVLAMSVESM READVYNVLR EALYEFPVLE
VNVNLPSWVM VLREDHWLRE SYQEAVRDTV KDIKRLRDVD RVVQQFAEYD FIEKAALAGI
EMGQGIAEID LYAPDELYDQ ILKEIVGVEI RGKDHLLQLM QDFAHAKAEY DQIADALKMV
KQTGYGIAAP ALSDMSLDEP EIIRQGSRFG VRLKAVAPSI HMIKVDVESE FAPIIGTEKQ
SEELVRYLMQ DFEDDPLSIW NSDIFGRSLS SIVREGIQAK LALMPENARY KLKETLERII
NEGSGGLIAI IL
//
