ID   E6BJJ0_ECOLX            Unreviewed;       388 AA.
AC   E6BJJ0;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Beta-lactamase {ECO:0000256|ARBA:ARBA00018879, ECO:0000256|RuleBase:RU361140};
DE            EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
GN   ORFNames=HMPREF9350_02532 {ECO:0000313|EMBL:EFU35465.1};
OS   Escherichia coli MS 85-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=679202 {ECO:0000313|EMBL:EFU35465.1, ECO:0000313|Proteomes:UP000005056};
RN   [1] {ECO:0000313|EMBL:EFU35465.1, ECO:0000313|Proteomes:UP000005056}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS 85-1 {ECO:0000313|EMBL:EFU35465.1,
RC   ECO:0000313|Proteomes:UP000005056};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein is a serine beta-lactamase with a substrate
CC       specificity for cephalosporins. {ECO:0000256|ARBA:ARBA00003808}.
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;
CC         Evidence={ECO:0000256|RuleBase:RU361140};
CC   -!- SIMILARITY: Belongs to the class-C beta-lactamase family.
CC       {ECO:0000256|ARBA:ARBA00007840, ECO:0000256|RuleBase:RU361140}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFU35465.1}.
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DR   EMBL; ADWQ01000009; EFU35465.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6BJJ0; -.
DR   MEROPS; S12.006; -.
DR   PATRIC; fig|679202.3.peg.2340; -.
DR   Proteomes; UP000005056; Unassembled WGS sequence.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0017001; P:antibiotic catabolic process; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR001466; Beta-lactam-related.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR001586; Beta-lactam_class-C_AS.
DR   PANTHER; PTHR46825:SF8; BETA-LACTAMASE-RELATED; 1.
DR   PANTHER; PTHR46825; D-ALANYL-D-ALANINE-CARBOXYPEPTIDASE/ENDOPEPTIDASE AMPH; 1.
DR   Pfam; PF00144; Beta-lactamase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   PROSITE; PS00336; BETA_LACTAMASE_C; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance {ECO:0000256|RuleBase:RU361140};
KW   Hydrolase {ECO:0000256|RuleBase:RU361140, ECO:0000313|EMBL:EFU35465.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..388
FT                   /note="Beta-lactamase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003201838"
FT   DOMAIN          40..387
FT                   /note="Beta-lactamase-related"
FT                   /evidence="ECO:0000259|Pfam:PF00144"
SQ   SEQUENCE   388 AA;  42823 MW;  2E20B0FA431E3597 CRC64;
     MAGRFVWKPD LMFKTTLCAL LITASCSTFA APQQINDIVH RTITPLIEQQ KIPGMAVAVI
     YQGKPYYFTW GYADIAKKQP VTQQTLFELG SVSKTFTGVL GGDAIARGEI KLSDPATKYW
     PELTAKQWNG ITLLHLATYT AGGLPLQVPD EVKSSSDLLR FYQNWQPAWA PGTQRLYANS
     SIGLFGALAV KPSGLSFEQA MQTRVFQPLK LNHTWINVPP PEEKNYAWGY REGKAVHVSP
     GALDAEAYGV KSTIEDMARW VRSNMNPRDI NDKTLQQGIQ LAQSRYWQTG DMYQGLGWEM
     LDWPVNPDSI INGSGNKIAL AAHPVKAITP PTPAVRASWV HKTGATSGFG SYVAFIPEKE
     LGIVMLANKN YPNPARVAAA WQILNALQ
//