ID A0A1I0VC53_9BACI Unreviewed; 492 AA.
AC A0A1I0VC53;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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 ORFNames=SAMN04488072_101310 {ECO:0000313|EMBL:SFA73633.1};
OS Lentibacillus halodurans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lentibacillus.
OX NCBI_TaxID=237679 {ECO:0000313|EMBL:SFA73633.1, ECO:0000313|Proteomes:UP000198642};
RN [1] {ECO:0000313|EMBL:SFA73633.1, ECO:0000313|Proteomes:UP000198642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.3702 {ECO:0000313|EMBL:SFA73633.1,
RC ECO:0000313|Proteomes:UP000198642};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FOJW01000001; SFA73633.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0VC53; -.
DR STRING; 237679.SAMN04488072_101310; -.
DR OrthoDB; 9761464at2; -.
DR Proteomes; UP000198642; 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 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:UP000198642};
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; 55603 MW; B435972910F954CA CRC64;
MERVDIFKDI SKRTNGDIYL GIVGAVRTGK STFIKHFMEL GVLPNISDES ERGRAHDELP
QSAAGKTIMT TEPKFIPNQA VSVHVDEGLD VNVRLVDCVG YAVDGAKGFE DENGPRMINT
PWYEDPIPFH DAAEIGTRKV IQEHSTIGVV VTTDGTFGEI ARTDYQEPEE KIVEEMKEVG
KPFIMVVNSA RPTSQETELL RQDLIDKYDI PVLAMNVETM TEHDVYNVMR EALYEFPVLE
VNVNLPSWVM VLNEEHWLQR NYQDAIQSTV KNIRRLRDVD HIIGNFADYD YIDRANLAGM
EMGDGIAEID LHAPDHLYDE VLKEIVGEEI RGKDHLLELM QDFAHAKREY DQVAGALQMV
KQTGYGIAAP TLEDMKLDEP EIIRQGSRFG VRLKAIAPSI HMVKVEVESE FAPIIGTEKQ
SEELVRYLMQ DFEEDPLSIW ESDIFGRSLS SIVREGIQAK ISLMPENARY KLKDTLERII
NEGSGGLIAI IL
//
