ALBF_BACSU
ID ALBF_BACSU Reviewed; 426 AA.
AC P71006;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Putative zinc protease AlbF;
DE EC=3.4.24.-;
DE AltName: Full=Antilisterial bacteriocin subtilosin biosynthesis protein AlbF;
GN Name=albF; Synonyms=ywhN; OrderedLocusNames=BSU37420;
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;
RX PubMed=9353933; DOI=10.1099/00221287-143-10-3313;
RA Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V.,
RA Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G.,
RA Kunst F., Danchin A., Glaser P.;
RT "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334
RT degrees).";
RL Microbiology 143:3313-3328(1997).
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.
RC STRAIN=168 / JH642, and 22a;
RX PubMed=10572140; DOI=10.1128/jb.181.23.7346-7355.1999;
RA Zheng G., Yan L.Z., Vederas J.C., Zuber P.;
RT "Genes of the sbo-alb locus of Bacillus subtilis are required for
RT production of the antilisterial bacteriocin subtilosin.";
RL J. Bacteriol. 181:7346-7355(1999).
RN [4]
RP FUNCTION.
RC STRAIN=168 / JH642;
RX PubMed=10809709; DOI=10.1128/jb.182.11.3266-3273.2000;
RA Zheng G., Hehn R., Zuber P.;
RT "Mutational analysis of the sbo-alb locus of Bacillus subtilis:
RT identification of genes required for subtilosin production and immunity.";
RL J. Bacteriol. 182:3266-3273(2000).
RN [5]
RP TRANSCRIPTIONAL REGULATION.
RC STRAIN=168 / JH642;
RX PubMed=10809710; DOI=10.1128/jb.182.11.3274-3277.2000;
RA Nakano M.M., Zheng G., Zuber P.;
RT "Dual control of sbo-alb operon expression by the Spo0 and ResDE systems of
RT signal transduction under anaerobic conditions in Bacillus subtilis.";
RL J. Bacteriol. 182:3274-3277(2000).
CC -!- FUNCTION: Required for production of the bacteriocin subtilosin. Could
CC catalyze some step in the processing of presubtilosin.
CC {ECO:0000269|PubMed:10572140, ECO:0000269|PubMed:10809709}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Divalent metal cations. Binds Zn(2+). {ECO:0000250};
CC -!- INDUCTION: Transcription is highly induced by oxygen limitation and is
CC under dual and independent control of Spo0A-AbrB and ResDE.
CC {ECO:0000269|PubMed:10809710}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
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DR EMBL; Z80360; CAB02504.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15769.1; -; Genomic_DNA.
DR PIR; E70058; E70058.
DR RefSeq; NP_391622.1; NC_000964.3.
DR RefSeq; WP_003242974.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P71006; -.
DR SMR; P71006; -.
DR IntAct; P71006; 9.
DR STRING; 224308.BSU37420; -.
DR MEROPS; M16.A16; -.
DR PaxDb; P71006; -.
DR PRIDE; P71006; -.
DR DNASU; 938515; -.
DR EnsemblBacteria; CAB15769; CAB15769; BSU_37420.
DR GeneID; 938515; -.
DR KEGG; bsu:BSU37420; -.
DR PATRIC; fig|224308.179.peg.4052; -.
DR eggNOG; COG0612; Bacteria.
DR OMA; FWHNGRN; -.
DR PhylomeDB; P71006; -.
DR BioCyc; BSUB:BSU37420-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: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 2: Evidence at transcript level;
KW Antibiotic biosynthesis; Bacteriocin biosynthesis; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Reference proteome; Zinc.
FT CHAIN 1..426
FT /note="Putative zinc protease AlbF"
FT /id="PRO_0000074408"
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 426 AA; 48982 MW; F6C43830BEAE3BF5 CRC64;
MEKKAFFQQL DERTDIRYTD SGLKIFRLKF PRAHLRLCNV KIDFGSRDVC IRAESGDTLL
PYGTAHFLEH LLFWHNGRNL YSDFFAHGAL LNAFTTYTDT NFMFTSLPDR LRQTIPILLD
ALWNHSFDKK IVAQEKAVIT SEIQTAHLNH QLSYHYQLIS MLSPSSPAAV FPAGRIEDIE
ALDISDLQKA YKAAYQAHRM TLFLIGGSEN TETLLPPHLQ LEKRPDYHAE RKIIPACPPV
LSQKMMLGDE ERMEDTWTGL QIGALPGQND LLSIKLYWDI AARILFQLDS PFFQEIQQTY
RLEIDRLSAE TYIYEDGGFL ILHSQGTHSS AYIDVASYYV TQKKEQVAAW LQYGKDSLTD
AIIYDSDYVR KCFEWAAECD RCDCSFLDMY HIIQDMDAQV FLSLIDAMAS SNKAIIHVSQ
KEAIRQ
