ID A0A1M6CQ77_9CLOT Unreviewed; 492 AA.
AC A0A1M6CQ77;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=SAMN02745176_00886 {ECO:0000313|EMBL:SHI63001.1};
OS Lutispora thermophila DSM 19022.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Lutispora.
OX NCBI_TaxID=1122184 {ECO:0000313|EMBL:SHI63001.1, ECO:0000313|Proteomes:UP000184442};
RN [1] {ECO:0000313|EMBL:SHI63001.1, ECO:0000313|Proteomes:UP000184442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19022 {ECO:0000313|EMBL:SHI63001.1,
RC ECO:0000313|Proteomes:UP000184442};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FQZS01000005; SHI63001.1; -; Genomic_DNA.
DR RefSeq; WP_073024940.1; NZ_FQZS01000005.1.
DR AlphaFoldDB; A0A1M6CQ77; -.
DR STRING; 1122184.SAMN02745176_00886; -.
DR OrthoDB; 9761464at2; -.
DR Proteomes; UP000184442; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000184442};
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"
FT COILED 336..363
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 492 AA; 56300 MW; C0396E93CADECD4A CRC64;
MEEFDLYRNI AERTEGSIYI GVVGPVRTGK STFIKRFMDL LVIPNIENEY KRDRTKDELP
QSANGRTIMT TEPKFVPNEA VEMTLEGNAK FKVRLVDCVG YLIEGAIGHM EDGNPRMVNT
PWFDNVIPFE DAAEIGTKKV INDHSTIGLV VTTDGTITDI PRRNYIQAEE RVINELKQIN
KPFVIILNSA KPDSQEAEEL RESLEVKYEM PVLLVDCLNM EMRDVDNILS KVLFEFPIRE
LNYHMPRWID SLENDHWLKK EIIDGILNST KDIYRIREVA SSTESLSVVD NLESASIRDM
DLARGTIDVR LNLKEGLFYR ILGEVSGYSI EGDYQLVSLM RDLSNAKKEY DKIKDAIKDV
KEVGYGVVAP SVDEIKLEEP EIVKHGGRFG VRLRASAPSL HIIKTNIETE VSPIVGTEKQ
SEEFIRYFMD EFESNPERIW ETNVFGKPLY DMVKEELQSK LYKMPDDIQG KMQLTLEKIV
NDTKGSIICI II
//
