ID   IMMA_BACSU              Reviewed;         169 AA.
AC   P96630; Q797K0;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Metallopeptidase ImmA;
DE            EC=3.4.-.-;
GN   Name=immA; Synonyms=ydcM; OrderedLocusNames=BSU04810;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Kasahara Y., Nakai S., Lee S., Sadaie Y., Ogasawara N.;
RT   "A 148 kbp sequence of the region between 35 and 47 degree of the Bacillus
RT   subtilis genome.";
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH IMMR.
RX   PubMed=18761623; DOI=10.1111/j.1365-2958.2008.06414.x;
RA   Bose B., Auchtung J.M., Lee C.A., Grossman A.D.;
RT   "A conserved anti-repressor controls horizontal gene transfer by
RT   proteolysis.";
RL   Mol. Microbiol. 70:570-582(2008).
CC   -!- FUNCTION: Involved in the regulation of horizontal gene transfer
CC       through the integrative and conjugative element ICEBs1. Required for
CC       degradation of the ICEBs1 repressor protein ImmR/YdcN.
CC       {ECO:0000269|PubMed:18761623}.
CC   -!- SUBUNIT: Interacts with ImmR. {ECO:0000269|PubMed:18761623}.
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DR   EMBL; AB001488; BAA19319.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12288.1; -; Genomic_DNA.
DR   PIR; B69774; B69774.
DR   RefSeq; NP_388362.1; NC_000964.3.
DR   RefSeq; WP_009966616.1; NZ_JNCM01000031.1.
DR   AlphaFoldDB; P96630; -.
DR   SMR; P96630; -.
DR   STRING; 224308.BSU04810; -.
DR   MEROPS; M78.001; -.
DR   PaxDb; P96630; -.
DR   EnsemblBacteria; CAB12288; CAB12288; BSU_04810.
DR   GeneID; 939924; -.
DR   KEGG; bsu:BSU04810; -.
DR   PATRIC; fig|224308.179.peg.511; -.
DR   eggNOG; COG2856; Bacteria.
DR   InParanoid; P96630; -.
DR   OMA; IHINERL; -.
DR   BioCyc; BSUB:BSU04810-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR010359; IrrE_HExxH.
DR   Pfam; PF06114; Peptidase_M78; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW   Zinc.
FT   CHAIN           1..169
FT                   /note="Metallopeptidase ImmA"
FT                   /id="PRO_0000360214"
FT   ACT_SITE        76
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         75
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         79
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   169 AA;  19401 MW;  9AF632343AD1B083 CRC64;
     MITIYTSKGI KHKVQSVIKT HGTNNVYEIC DIQKIYILKN DLGQANGLLQ HDKATDQYLI
     HINENLQHQQ FVIAHELGHY FLHKRLNTFK VVNCSKVLKD KLEHQASLFA SELILTDKML
     NEALPYIQGF SKEQIAAYFN VPSFVTDYKL SQIGSFSNRI YSHEISAFG