ID   BLAC_BACSU              Reviewed;         306 AA.
AC   P39824; O34848;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   27-MAR-2024, entry version 131.
DE   RecName: Full=Beta-lactamase;
DE            EC=3.5.2.6;
DE   AltName: Full=Penicillinase;
DE   Flags: Precursor;
GN   Name=penP; OrderedLocusNames=BSU18800;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / 6GM;
RA   van Dijl J.M., de Jong A., Nauta A., Venema G., Bron S.;
RT   "Identification of penicillinase-encoding genes of Bacillus
RT   amyloliquefaciens and Bacillus subtilis.";
RL   Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT   "Sequence analysis of the Bacillus subtilis chromosome region between the
RT   terC and odhAB loci cloned in a yeast artificial chromosome.";
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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   [4]
RP   PROTEIN SEQUENCE OF 37-47, AND SUBCELLULAR LOCATION.
RC   STRAIN=168;
RX   PubMed=10658653; DOI=10.1099/00221287-146-1-65;
RA   Hirose I., Sano K., Shioda I., Kumano M., Nakamura K., Yamane K.;
RT   "Proteome analysis of Bacillus subtilis extracellular proteins: a two-
RT   dimensional protein electrophoretic study.";
RL   Microbiology 146:65-75(2000).
CC   -!- FUNCTION: This protein is a beta-lactamase with a substrate specificity
CC       for penicillins.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a beta-lactam + H2O = a substituted beta-amino acid;
CC         Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627,
CC         ChEBI:CHEBI:140347; EC=3.5.2.6; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10101};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10658653}.
CC   -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC       {ECO:0000305}.
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DR   EMBL; Z35652; CAA84711.1; -; Genomic_DNA.
DR   EMBL; AF027868; AAB84426.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13772.1; -; Genomic_DNA.
DR   PIR; G69674; G69674.
DR   RefSeq; NP_389761.1; NC_000964.3.
DR   RefSeq; WP_003231385.1; NZ_JNCM01000036.1.
DR   PDB; 6W2Z; X-ray; 1.50 A; A/B=34-306.
DR   PDBsum; 6W2Z; -.
DR   AlphaFoldDB; P39824; -.
DR   SMR; P39824; -.
DR   STRING; 224308.BSU18800; -.
DR   PaxDb; 224308-BSU18800; -.
DR   EnsemblBacteria; CAB13772; CAB13772; BSU_18800.
DR   GeneID; 940129; -.
DR   KEGG; bsu:BSU18800; -.
DR   PATRIC; fig|224308.179.peg.2049; -.
DR   eggNOG; COG2367; Bacteria.
DR   InParanoid; P39824; -.
DR   OrthoDB; 9784149at2; -.
DR   PhylomeDB; P39824; -.
DR   BioCyc; BSUB:BSU18800-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR045155; Beta-lactam_cat.
DR   InterPro; IPR000871; Beta-lactam_class-A.
DR   InterPro; IPR023650; Beta-lactam_class-A_AS.
DR   PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR   PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF13354; Beta-lactamase2; 1.
DR   PRINTS; PR00118; BLACTAMASEA.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   PROSITE; PS00146; BETA_LACTAMASE_A; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic resistance; Direct protein sequencing; Hydrolase;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000269|PubMed:10658653"
FT   CHAIN           37..306
FT                   /note="Beta-lactamase"
FT                   /id="PRO_0000016975"
FT   ACT_SITE        89
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10101"
FT   BINDING         251..253
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        51
FT                   /note="K -> N (in Ref. 1; CAA84711)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        97..99
FT                   /note="AAV -> GGF (in Ref. 1; CAA84711)"
FT                   /evidence="ECO:0000305"
FT   HELIX           48..60
FT                   /evidence="ECO:0007829|PDB:6W2Z"
FT   STRAND          63..70
FT                   /evidence="ECO:0007829|PDB:6W2Z"
FT   TURN            71..73
FT                   /evidence="ECO:0007829|PDB:6W2Z"
FT   STRAND          76..80
FT                   /evidence="ECO:0007829|PDB:6W2Z"
FT   HELIX           88..90
FT                   /evidence="ECO:0007829|PDB:6W2Z"
FT   HELIX           91..102
FT                   /evidence="ECO:0007829|PDB:6W2Z"
FT   HELIX           105..109
FT                   /evidence="ECO:0007829|PDB:6W2Z"
FT   STRAND          110..112
FT                   /evidence="ECO:0007829|PDB:6W2Z"
FT   HELIX           116..118
FT                   /evidence="ECO:0007829|PDB:6W2Z"
FT   HELIX           126..129
FT                   /evidence="ECO:0007829|PDB:6W2Z"
FT   TURN            130..132
FT                   /evidence="ECO:0007829|PDB:6W2Z"
FT   HELIX           136..146
FT                   /evidence="ECO:0007829|PDB:6W2Z"
FT   HELIX           149..158
FT                   /evidence="ECO:0007829|PDB:6W2Z"
FT   HELIX           161..171
FT                   /evidence="ECO:0007829|PDB:6W2Z"
FT   HELIX           185..187
FT                   /evidence="ECO:0007829|PDB:6W2Z"
FT   HELIX           200..211
FT                   /evidence="ECO:0007829|PDB:6W2Z"
FT   HELIX           218..228
FT                   /evidence="ECO:0007829|PDB:6W2Z"
FT   HELIX           232..234
FT                   /evidence="ECO:0007829|PDB:6W2Z"
FT   TURN            235..237
FT                   /evidence="ECO:0007829|PDB:6W2Z"
FT   HELIX           238..241
FT                   /evidence="ECO:0007829|PDB:6W2Z"
FT   STRAND          247..255
FT                   /evidence="ECO:0007829|PDB:6W2Z"
FT   TURN            256..258
FT                   /evidence="ECO:0007829|PDB:6W2Z"
FT   STRAND          259..267
FT                   /evidence="ECO:0007829|PDB:6W2Z"
FT   STRAND          274..281
FT                   /evidence="ECO:0007829|PDB:6W2Z"
FT   HELIX           291..304
FT                   /evidence="ECO:0007829|PDB:6W2Z"
SQ   SEQUENCE   306 AA;  33446 MW;  95BE5644B731500E CRC64;
     MKLKTKASIK FGICVGLLCL SITGFTPFFN STHAEAKSIE DTNMASCITN KKFVQLEKKF
     DARLGVYAID IGSNKTIAYR PNERFAYAST YKVLAAAAVL KKNSIEKLNE VIHYSKDDLV
     TYSPITEKHL DTGMSLKEIS EAAIRYSDNT AGNILLQQLG GPKGFEKSLK QIGDHVTKAK
     RFETDLNSAI PGDIRDTSTA KALATDLKAF TLDNTLTTDK RMILTDWMRG NATGDELIRA
     GAPIGWEVGD KSGAGSYGTR NDIAIVWPPN RAPIVVAILS NRFTKDANYD NALIAEAAKV
     VLNDLK
//