ID   ALBF_BACIU              Reviewed;         427 AA.
AC   Q8RKH2;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Putative zinc protease AlbF;
DE            EC=3.4.24.-;
DE   AltName: Full=Antilisterial bacteriocin subtilosin biosynthesis protein AlbF;
GN   Name=albF;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 6633 / PCI 219 / NRS 231;
RA   Stein T., Duesterhus S., Entian K.-D.;
RT   "Subtilosin A biosynthesis is conserved among two different classes of
RT   Bacillus subtilis strains.";
RL   Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for production of the bacteriocin subtilosin. Could
CC       catalyze some step in the processing of presubtilosin (By similarity).
CC       {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Divalent metal cations. Binds Zn(2+). {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
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DR   EMBL; AJ430547; CAD23204.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8RKH2; -.
DR   SMR; Q8RKH2; -.
DR   MEROPS; M16.A16; -.
DR   PRIDE; Q8RKH2; -.
DR   PATRIC; fig|1423.172.peg.2479; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030152; P:bacteriocin biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   SUPFAM; SSF63411; SSF63411; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; Bacteriocin biosynthesis; Hydrolase;
KW   Metal-binding; Metalloprotease; Protease; Zinc.
FT   CHAIN           1..427
FT                   /note="Putative zinc protease AlbF"
FT                   /id="PRO_0000074409"
FT   ACT_SITE        69
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         70
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   427 AA;  49068 MW;  7D2C7EACAF9EDC41 CRC64;
     MEKKAFFQQL DERTDIRYTD SGMKIIRLKF PRAHLRLCNV KIDFGSRDVC LQAESGDTLL
     PYGTAHFLEH LLFWHNGRNL YTDFFAHGAL LNAFTTYTDT NFMFTSLPDR LRQTIPILLD
     ALWNHSFDKK MITQEKAVIT SEIQTAHLNH QLYYHYQLIS MLSPASPAAV FPAGRIEDIE
     ALDIRDLQKA YNAAYQPQRM TLFLIGGSED TEALLPPHLR LEKRPNHKAE RKIISACPPP
     ALSQKMVLGN EERIEDTWTG LQVGAIPGQN NLLTLKLYWD IASRILFQLD SPFFQEIQQT
     YRLEIDCLSA EAHMYEDGGF LILHSQGAHS SAYIDVASYY VTQQKQQIET WLQYGKDSLT
     DAIIYDSDYV RKCFEWAAEC DRCDCTFLDM YRIIHDMNSQ DFLSLIDALA SSKKAVIHVS
     QKEAIGQ