ID   SP4A_BACAN              Reviewed;         492 AA.
AC   Q81SW4; E9QV53; E9QV54; Q6I143; Q6KUZ7;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Stage IV sporulation protein A {ECO:0000312|EMBL:AAP25467.1};
DE            EC=3.6.1.- {ECO:0000250|UniProtKB:P35149};
DE   AltName: Full=Coat morphogenetic protein SpoIVA {ECO:0000303|PubMed:17114257};
GN   Name=spoIVA {ECO:0000312|EMBL:AAP25467.1};
GN   OrderedLocusNames=BA_1530, BAS1419, GBAA_1530;
OS   Bacillus anthracis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1392;
RN   [1] {ECO:0000312|EMBL:AAP25467.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames / isolate Porton {ECO:0000312|EMBL:AAP25467.1};
RX   PubMed=12721629; DOI=10.1038/nature01586;
RA   Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA   Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA   Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA   Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA   DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA   Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA   Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA   Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA   White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA   Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT   "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT   related bacteria.";
RL   Nature 423:81-86(2003).
RN   [2] {ECO:0000312|EMBL:AAT30628.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames ancestor {ECO:0000312|EMBL:AAT30628.2};
RX   PubMed=18952800; DOI=10.1128/jb.01347-08;
RA   Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA   Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT   "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL   J. Bacteriol. 191:445-446(2009).
RN   [3] {ECO:0000312|EMBL:AAT53739.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sterne {ECO:0000312|EMBL:AAT53739.1};
RA   Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA   Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA   Richardson P., Rubin E., Tice H.;
RT   "Complete genome sequence of Bacillus anthracis Sterne.";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000305}
RP   FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=17114257; DOI=10.1128/jb.00921-06;
RA   Giorno R., Bozue J., Cote C., Wenzel T., Moody K.S., Mallozzi M., Ryan M.,
RA   Wang R., Zielke R., Maddock J.R., Friedlander A., Welkos S., Driks A.;
RT   "Morphogenesis of the Bacillus anthracis spore.";
RL   J. Bacteriol. 189:691-705(2007).
CC   -!- FUNCTION: ATPase. Has a role at an early stage in the morphogenesis of
CC       the spore coat outer layers. Directs the assembly of the coat and
CC       exosporium to an area around the forespore.
CC       {ECO:0000250|UniProtKB:P35149, ECO:0000269|PubMed:17114257}.
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:0000250|UniProtKB:P35149};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P35149}.
CC       Note=Localized on spore coat surrounding the forespore.
CC       {ECO:0000250|UniProtKB:P35149}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in early onset of sporulation.
CC       {ECO:0000269|PubMed:17114257}.
CC   -!- DISRUPTION PHENOTYPE: Defective in formation of mature forespores.
CC       Fails to progress beyond very early stages of sporulation. Forespores
CC       lack the germ cell wall or cortex and the mother cells are filled with
CC       swirls of electron-dense material. {ECO:0000269|PubMed:17114257}.
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DR   EMBL; AE016879; AAP25467.1; -; Genomic_DNA.
DR   EMBL; AE017334; AAT30628.2; -; Genomic_DNA.
DR   EMBL; AE017225; AAT53739.1; -; Genomic_DNA.
DR   RefSeq; NP_843981.1; NC_003997.3.
DR   RefSeq; WP_000416519.1; NZ_WXXJ01000020.1.
DR   RefSeq; YP_027688.1; NC_005945.1.
DR   AlphaFoldDB; Q81SW4; -.
DR   IntAct; Q81SW4; 6.
DR   STRING; 261594.GBAA_1530; -.
DR   DNASU; 1087217; -.
DR   EnsemblBacteria; AAP25467; AAP25467; BA_1530.
DR   EnsemblBacteria; AAT30628; AAT30628; GBAA_1530.
DR   GeneID; 59158208; -.
DR   GeneID; 64203047; -.
DR   GeneID; 67506211; -.
DR   KEGG; ban:BA_1530; -.
DR   KEGG; bar:GBAA_1530; -.
DR   KEGG; bat:BAS1419; -.
DR   PATRIC; fig|198094.11.peg.1502; -.
DR   eggNOG; COG0699; Bacteria.
DR   HOGENOM; CLU_043635_0_0_9; -.
DR   OMA; RMPENAQ; -.
DR   Proteomes; UP000000427; Chromosome.
DR   Proteomes; UP000000594; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042601; C:endospore-forming forespore; ISS:UniProtKB.
DR   GO; GO:0031160; C:spore wall; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR   GO; GO:0070499; P:exosporium assembly; IDA:UniProtKB.
DR   GO; GO:0042244; P:spore wall assembly; IMP:UniProtKB.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IDA:UniProtKB.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014201; Spore_IV_A.
DR   Pfam; PF09547; Spore_IV_A; 1.
DR   PIRSF; PIRSF007466; SpoIVA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR02836; spore_IV_A; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Hydrolase; Nucleotide-binding; Reference proteome;
KW   Sporulation.
FT   CHAIN           1..492
FT                   /note="Stage IV sporulation protein A"
FT                   /id="PRO_0000422237"
FT   MOTIF           24..31
FT                   /note="Walker A motif; involved in ATP-binding"
FT                   /evidence="ECO:0000255, ECO:0000305"
FT   BINDING         24..31
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P35149"
SQ   SEQUENCE   492 AA;  55613 MW;  B9964465278D4137 CRC64;
     MEKVDIFKDI AERTGGDIYF GVVGAVRTGK STFIKKFMEL VVIPNIENES DRQRAQDELP
     QSAAGRTIMT TEPKFVPNQA VSIEVDEGLE VNIRLVDCVG YTVPGAKGYE DENGPRMINT
     PWYEEPIPFH EAAEIGTRKV IQEHSTIGVV ITTDGTIGEI PRRDYIEAEE RVVNELKEVG
     KPFIMIINTV QPYHPDTEQL RQSLSEEYDI PVIAMSVESL RETDVYNVLR EALFEFPVLE
     VNVNLPSWVM VLNEGHWLRQ SYQEAVQETV KDIKRLRDVD RVVWQFSQYE FIDRASLAGI
     DMGQGVAEID LYAPDELYDQ ILKEVVGVEI RGKDHLLKLM LDLSHAKIEY DQVADALRMV
     KQTGYGVAAP ALADMSLDEP EIIRHGSRFG VKLKAVAPSI HMIKVDVEST FEPIIGTEKQ
     SEELVRYLMQ DFEDDPLSIW NSDIFGRSLS SIVREGIQAK LSLMPENARY KLKETLERII
     NEGSGGLIAI IL