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Database: UniProt
Entry: D9S2W5_THEOJ
LinkDB: D9S2W5_THEOJ
Original site: D9S2W5_THEOJ 
ID   D9S2W5_THEOJ            Unreviewed;       492 AA.
AC   D9S2W5;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 59.
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   OrderedLocusNames=Toce_0980 {ECO:0000313|EMBL:ADL07742.1};
OS   Thermosediminibacter oceani (strain ATCC BAA-1034 / DSM 16646 /
OS   JW/IW-1228P).
OC   Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC   Thermosediminibacteraceae; Thermosediminibacter.
OX   NCBI_TaxID=555079 {ECO:0000313|EMBL:ADL07742.1, ECO:0000313|Proteomes:UP000000272};
RN   [1] {ECO:0000313|EMBL:ADL07742.1, ECO:0000313|Proteomes:UP000000272}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1034 / DSM 16646 / JW/IW-1228P
RC   {ECO:0000313|Proteomes:UP000000272};
RX   PubMed=21304740;
RA   Pitluck S., Yasawong M., Munk C., Nolan M., Lapidus A., Lucas S.,
RA   Glavina Del Rio T., Tice H., Cheng J.F., Bruce D., Detter C., Tapia R.,
RA   Han C., Goodwin L., Liolios K., Ivanova N., Mavromatis K., Mikhailova N.,
RA   Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Rohde M., Spring S., Sikorski J., Goker M., Woyke T.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Thermosediminibacter oceani type strain
RT   (JW/IW-1228P).";
RL   Stand. Genomic Sci. 3:108-116(2010).
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; CP002131; ADL07742.1; -; Genomic_DNA.
DR   RefSeq; WP_013275784.1; NC_014377.1.
DR   AlphaFoldDB; D9S2W5; -.
DR   STRING; 555079.Toce_0980; -.
DR   KEGG; toc:Toce_0980; -.
DR   eggNOG; COG0370; Bacteria.
DR   HOGENOM; CLU_043635_0_0_9; -.
DR   OrthoDB; 9761464at2; -.
DR   Proteomes; UP000000272; 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:UP000000272};
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;  55688 MW;  723265A3F3A36618 CRC64;
     MEKFDLFKDI AERTGGDIYI GVVGPVRAGK STFVKKFMEL LVIPNIQDPN ARVRAKDELP
     QSGAGRTITT AEPKFIPSQA VEITFKDNIK FRVRLVDNVG FSVKGALGYE DENGPRMVST
     PWFDEEIPFQ EAAEIGTRKV IEEHSTIGVV VTTDGTITDI PRENYVDAEE RVVNELKAIG
     KPFVIVLNSI NPSSESTLEL KEELESKYDV PVLPLDCQAM TQKDIYALLE QILYEFPLME
     INIHIPKWVE VLEKEHWLRQ QFEKTVKETV KDIHRVRDIE RIVTDLGASD FLERVEIKEM
     NLGTGTADLN LEAKKDLFYK VLSELSGLTI EGDHHLMSLM KDLTKAKKEY DKVAKALDDV
     KKVGYGIVPP QLDELTLEEP EIIRQGSRFG VRIRAIAPSI HMIRADIQTE ISPIIGTEKQ
     SEELISYLMS EFENDPEKIW QTNIFGKSLQ DLVREGIQNK LLHMPEAAQS KLQETLQRIV
     NEGSGSLICI IL
//
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