ID H6NAG1_9BACL Unreviewed; 492 AA.
AC H6NAG1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 39.
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=PM3016_3018 {ECO:0000313|EMBL:AFC29886.1};
OS Paenibacillus mucilaginosus 3016.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1116391 {ECO:0000313|EMBL:AFC29886.1, ECO:0000313|Proteomes:UP000007523};
RN [1] {ECO:0000313|EMBL:AFC29886.1, ECO:0000313|Proteomes:UP000007523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3016 {ECO:0000313|EMBL:AFC29886.1,
RC ECO:0000313|Proteomes:UP000007523};
RX PubMed=22535950; DOI=10.1128/JB.00323-12;
RA Ma M., Wang Z., Li L., Jiang X., Guan D., Cao F., Chen H., Wang X.,
RA Shen D., Du B., Li J.;
RT "Complete Genome Sequence of Paenibacillus mucilaginosus 3016, a Bacterium
RT Functional as Microbial Fertilizer.";
RL J. Bacteriol. 194:2777-2778(2012).
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; CP003235; AFC29886.1; -; Genomic_DNA.
DR RefSeq; WP_013916497.1; NC_016935.1.
DR AlphaFoldDB; H6NAG1; -.
DR STRING; 1116391.PM3016_3018; -.
DR KEGG; pmq:PM3016_3018; -.
DR HOGENOM; CLU_043635_0_0_9; -.
DR Proteomes; UP000007523; 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:UP000007523};
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; 55196 MW; BFE31DBF1C82F4E4 CRC64;
MEKVDIFKDI AERTGGDIYL GVVGAVRTGK STFIKRFMES VVLPNIQNES DRVRATDELP
QSAAGRTIMT TEPKFVPNTA VQLHVAEGLN VNVRLVDCVG YVVEGAKGYE DESGPRMINT
PWFDEAIPFQ EAAEIGTRKV IQEHATLGVV ITTDGSIAEI PRSSYVEAED RIIGELKEVG
KPFIVIVNST KPQSDAVQEL RSELQEKHDV PVVAMSVASM NEDDMTSVLR EVLYEFPVHE
VNVNLPSWVM VLEENHWLRS SFENSVRETV QDIRRLRDVD RVVGSFEQYE FIDKAALAGM
NMGQGVAEID LYAPDELYDR ILMEVVGVEI RGKDHLLQLM QEFTHAKREY DHFAEALEMV
KTTGYGIAPP TLAEMALDEP ELIRQGSRFG VRLKATAPSI HMIRVDVESE FSPIIGTEKQ
SEELVRYLMQ DFEDNPLKIW ESDIFGRSLH SIVREGIQGK LAMMPDNARY KLQETLGRII
NEGSGGLIAI IL
//
