BLAC_BACSU
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 03-AUG-2022, entry version 124.
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; Firmicutes; 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; P39824; -.
DR PRIDE; P39824; -.
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 OMA; EWMKGNA; -.
DR PhylomeDB; P39824; -.
DR BioCyc; BSUB:BSU18800-MON; -.
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; -; 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; PTHR35333; 1.
DR Pfam; PF13354; Beta-lactamase2; 1.
DR PRINTS; PR00118; BLACTAMASEA.
DR SUPFAM; SSF56601; SSF56601; 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
