ID   SP4A_CLOD6              Reviewed;         491 AA.
AC   Q182W3;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 2.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Stage IV sporulation protein A {ECO:0000312|EMBL:CAJ69515.2};
DE            EC=3.6.1.- {ECO:0000250|UniProtKB:P35149};
DE   AltName: Full=Coat morphogenetic protein SpoIVA {ECO:0000303|PubMed:23292781};
GN   Name=spoIVA {ECO:0000312|EMBL:CAJ69515.2}; OrderedLocusNames=CD630_26290;
OS   Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=272563;
RN   [1] {ECO:0000312|EMBL:CAJ69515.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=630 {ECO:0000312|EMBL:CAJ69515.2};
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA   Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT   mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(2006).
RN   [2] {ECO:0000305}
RP   FUNCTION, INTERACTION WITH SIPL, SUBCELLULAR LOCATION, DISRUPTION
RP   PHENOTYPE, AND MUTAGENESIS OF LYS-35.
RC   STRAIN=630 {ECO:0000269|PubMed:23292781};
RX   PubMed=23292781; DOI=10.1128/jb.02181-12;
RA   Putnam E.E., Nock A.M., Lawley T.D., Shen A.;
RT   "SpoIVA and SipL are Clostridium difficile spore morphogenetic proteins.";
RL   J. Bacteriol. 195:1214-1225(2013).
CC   -!- FUNCTION: ATPase. Has a role at an early stage in the morphogenesis of
CC       the spore coat and is required for proper coat localization to the
CC       forespore. {ECO:0000250|UniProtKB:P35149, ECO:0000269|PubMed:23292781}.
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   -!- SUBUNIT: Interacts (via Walker A motif) with SipL (via C-terminus LysM
CC       domain). {ECO:0000269|PubMed:23292781}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P35149}.
CC       Note=Localized on spore coat surrounding the forespore.
CC       {ECO:0000250|UniProtKB:P35149, ECO:0000269|PubMed:23292781}.
CC   -!- DISRUPTION PHENOTYPE: Sporulation defects. Defects in proper coat
CC       localization around the forespore, but not in cortex formation.
CC       {ECO:0000269|PubMed:23292781}.
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DR   EMBL; AM180355; CAJ69515.2; -; Genomic_DNA.
DR   RefSeq; WP_004454943.1; NZ_CP010905.2.
DR   RefSeq; YP_001089140.2; NC_009089.1.
DR   AlphaFoldDB; Q182W3; -.
DR   STRING; 272563.CD630_26290; -.
DR   EnsemblBacteria; CAJ69515; CAJ69515; CD630_26290.
DR   GeneID; 66355027; -.
DR   KEGG; cdf:CD630_26290; -.
DR   KEGG; pdc:CDIF630_02883; -.
DR   PATRIC; fig|272563.120.peg.2772; -.
DR   eggNOG; COG0699; Bacteria.
DR   OMA; RMPENAQ; -.
DR   PhylomeDB; Q182W3; -.
DR   BioCyc; PDIF272563:G12WB-2780-MON; -.
DR   Proteomes; UP000001978; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042601; C:endospore-forming forespore; IMP:UniProtKB.
DR   GO; GO:0031160; C:spore wall; IMP:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR   GO; GO:0034301; P:endospore formation; IMP:CACAO.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP: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   1: Evidence at protein level;
KW   ATP-binding; Coiled coil; Cytoplasm; Hydrolase; Nucleotide-binding;
KW   Reference proteome; Sporulation.
FT   CHAIN           1..491
FT                   /note="Stage IV sporulation protein A"
FT                   /id="PRO_0000422238"
FT   COILED          334..362
FT                   /evidence="ECO:0000255"
FT   MOTIF           23..30
FT                   /note="Walker A motif; involved in ATP-binding"
FT                   /evidence="ECO:0000255, ECO:0000305"
FT   BINDING         23..30
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P35149"
FT   MUTAGEN         35
FT                   /note="K->E: Reduced binding to SipL."
FT                   /evidence="ECO:0000269|PubMed:23292781"
SQ   SEQUENCE   491 AA;  55517 MW;  9114C3574BED7554 CRC64;
     MNNNIYEDIS KRTQGDIYIG VVGPVRTGKS TFIRKFMEKL VIPNIDNEFK KDRTRDEIPQ
     SGSGKTIMTV EPKFVPADGV EIKIKDTVSL KVRMVDCVGY IVEGALGHEE GGKQRLVSTP
     WSQEAMTFEK AAEIGTKKVI KDHSTIGIVV LTDGSVTGID RKSYVEPEER VIQELKNLKK
     PFAVVLNTLS PKSEETSMLR SELEEKYEVP VLPMNVVEME EEDIEEVMEA VLYDFPLTEI
     RINLPKWVEG LERNHWIKSS IITTLKQSII DIGKIRDIEG IIQGFSELEF LEDTGVDNVE
     LGEGVINIDL QTKQDLFYNV LEEKSGFKIE GDYQLLSLIT RLSKVKNEYD KIESALIDAK
     IKGYGVVAPS LEELSLEEPE IMKQGKQYGI KLKANAPSLH IIKADISTEV SPIVGNQNQG
     EEMIKYLMEV FEEQPADLWE SNMFGKSLHD LVKEQLQSKL YTMPEEIRVK MQKTLQKIVN
     EGSSNIITIL L