ID A0A162UYQ3_9CLOT Unreviewed; 492 AA.
AC A0A162UYQ3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
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:KZL94421.1};
GN ORFNames=CLMAG_14740 {ECO:0000313|EMBL:KZL94421.1};
OS Clostridium magnum DSM 2767.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121326 {ECO:0000313|EMBL:KZL94421.1, ECO:0000313|Proteomes:UP000076603};
RN [1] {ECO:0000313|EMBL:KZL94421.1, ECO:0000313|Proteomes:UP000076603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2767 {ECO:0000313|EMBL:KZL94421.1,
RC ECO:0000313|Proteomes:UP000076603};
RA Poehlein A., Uhlig R., Fischer R., Bahl H., Daniel R.;
RT "Genome sequence of Clostridium magnum DSM 2767.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:KZL94421.1}.
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DR EMBL; LWAE01000001; KZL94421.1; -; Genomic_DNA.
DR RefSeq; WP_066619921.1; NZ_LWAE01000001.1.
DR AlphaFoldDB; A0A162UYQ3; -.
DR STRING; 1121326.CLMAG_14740; -.
DR PATRIC; fig|1121326.3.peg.1446; -.
DR OrthoDB; 9761464at2; -.
DR Proteomes; UP000076603; Unassembled WGS sequence.
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, ECO:0000313|EMBL:KZL94421.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR007466};
KW Reference proteome {ECO:0000313|Proteomes:UP000076603};
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 238..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; 56054 MW; B34DACEA69EA3F8A CRC64;
MENFDIYKDI AERTQGDIYV GVVGPVRTGK STFIKRFMEL MVIPNIENSY KKQRAKDELP
QSSSGKSIHT TEPKFVPNEA IEISLNENTK FKVRLVDCVG YIVKNSQGYM EGDKAKMVTT
PWYDYEIPFE EAAEIGTKKV INEHSTIGLL VTTDGSITDI SREDYVEAEE RVVNELKAIN
KPFIIVLNSQ QPNSEDAILL KNELEEKYDV PVQGMDVLNM KEEDITDVFQ RILKEFPIKE
INIDMPEWIE KLEPSHWLKL DFFELVKNMC KSVYKVRDIG KSVKGFEEVD FMGDSNITEI
NMGEGTARIN LKPKHDLFYK ILGEVCGTEL GGESDLLNIV KEMHKAKVEY DKVADALRDV
RETGYGLVAP QLSEMKLEEP QIVRQGNRTG VKLKASAPSL HFIRADIETE VSPIMGTERE
SEEMVKSLFE QFESDPSKIW QSNMFGKSLE ILVKEGLQNK LYKMPEDVQI KIQKTLQKII
NEGNGGLICI IL
//
