ID Q67NS4_SYMTH Unreviewed; 493 AA.
AC Q67NS4;
DT 11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 82.
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:BAD40669.1};
GN OrderedLocusNames=STH1684 {ECO:0000313|EMBL:BAD40669.1};
OS Symbiobacterium thermophilum (strain T / IAM 14863).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC Symbiobacterium.
OX NCBI_TaxID=292459 {ECO:0000313|EMBL:BAD40669.1, ECO:0000313|Proteomes:UP000000417};
RN [1] {ECO:0000313|EMBL:BAD40669.1, ECO:0000313|Proteomes:UP000000417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T / IAM 14863 {ECO:0000313|Proteomes:UP000000417};
RX PubMed=15383646; DOI=10.1093/nar/gkh830;
RA Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K.,
RA Ikeda H., Hattori M., Beppu T.;
RT "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium
RT that depends on microbial commensalism.";
RL Nucleic Acids Res. 32:4937-4944(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; AP006840; BAD40669.1; -; Genomic_DNA.
DR RefSeq; WP_011195812.1; NC_006177.1.
DR AlphaFoldDB; Q67NS4; -.
DR STRING; 292459.STH1684; -.
DR KEGG; sth:STH1684; -.
DR eggNOG; COG0699; Bacteria.
DR HOGENOM; CLU_043635_0_0_9; -.
DR OrthoDB; 9761464at2; -.
DR Proteomes; UP000000417; 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 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:UP000000417};
KW Sporulation {ECO:0000256|PIRNR:PIRNR007466}.
FT DOMAIN 1..238
FT /note="Stage IV sporulation protein A ATPase"
FT /evidence="ECO:0000259|Pfam:PF09547"
FT DOMAIN 239..417
FT /note="Stage IV sporulation protein A middle"
FT /evidence="ECO:0000259|Pfam:PF20438"
FT DOMAIN 418..493
FT /note="Sporulation stage IV protein A C-terminal"
FT /evidence="ECO:0000259|Pfam:PF20439"
FT COILED 337..364
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 493 AA; 55296 MW; A4706A6040D6ACAB CRC64;
MERIDIFEDV ARRTGGDIYI GVVGPVRTGK STFIRRLAEQ VILPNIEDEY LQARIRDELP
QSGNGRTIMT VEPKFVPDEA VEITLREGLT VRVRLVDSVG YAVEGALGYM QEDGSPRMVR
TPWFEEEIPF HDAAEIGTRK VIAEHSTIGL LVTTDGTITD LARGKYLEAE ERVVSELQAL
GKPFVIVLNT TRPYAQETME LAGELEVKYN APVIPVDASE LTQDDIHLIL EQALFEFPVR
EANIALPRWV EELDSAHPVR AQFEEAIAEA LQGIQKIRDV DAAVERLSSY EFMAAVNLQS
IDMGAGVAHV QTEARDDLYY QVLEEITGVP LEGKHTMVRL LREYTQAKRE YDKIKDALED
VKATGYGVVT PAIEDITFEE PELVRQGIMY GVKLQATAPS LHFIRADISA EVTPIIGTAK
QGEELVQYLL ERFEDDPRQL WEFDIFGKSL HELVQEGIKA KLHRMPEDAQ VKLQETLSRI
INEGSGGLIC III
//
