ID A0A127VCV7_9SPHI Unreviewed; 454 AA.
AC A0A127VCV7;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Beta-lactamase {ECO:0000256|ARBA:ARBA00018879, ECO:0000256|RuleBase:RU361140};
DE EC=3.5.2.6 {ECO:0000256|RuleBase:RU361140};
GN ORFNames=AY601_2298 {ECO:0000313|EMBL:AMP99192.1};
OS Pedobacter cryoconitis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=188932 {ECO:0000313|EMBL:AMP99192.1, ECO:0000313|Proteomes:UP000071561};
RN [1] {ECO:0000313|EMBL:AMP99192.1, ECO:0000313|Proteomes:UP000071561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 27485 {ECO:0000313|EMBL:AMP99192.1,
RC ECO:0000313|Proteomes:UP000071561};
RA Lee J., Kim O.-S.;
RT "Complete genome sequence of Pedobacter cryoconitis PAMC 27485.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP014504; AMP99192.1; -; Genomic_DNA.
DR RefSeq; WP_068400816.1; NZ_CP014504.1.
DR AlphaFoldDB; A0A127VCV7; -.
DR KEGG; pcm:AY601_2298; -.
DR PATRIC; fig|188932.3.peg.2406; -.
DR OrthoDB; 9793489at2; -.
DR Proteomes; UP000071561; Chromosome.
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; D-ALANYL-D-ALANINE-CARBOXYPEPTIDASE/ENDOPEPTIDASE AMPH; 1.
DR PANTHER; PTHR46825:SF9; PROTEIN FLP; 1.
DR Pfam; PF00144; Beta-lactamase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR PROSITE; PS00336; BETA_LACTAMASE_C; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|RuleBase:RU361140};
KW Hydrolase {ECO:0000256|RuleBase:RU361140};
KW Reference proteome {ECO:0000313|Proteomes:UP000071561}.
FT DOMAIN 142..443
FT /note="Beta-lactamase-related"
FT /evidence="ECO:0000259|Pfam:PF00144"
SQ SEQUENCE 454 AA; 52106 MW; 4ACECFB2F29E1D13 CRC64;
MNPEQMIIQL AGFYNHDQFS EIYLLHADEF KQHVAEKTVM DFYHYDLKRS LGEITSWEFI
KTEQEVAEYL INFKYGELSL KIALTADDLL ALVNWEPVHQ EEEILNIRDP LTILSTNRLT
TPLQCFIDQQ AIKYLQDPNN RSLSIGLIRG THTETFFYGE THLDNHTLPD SHSLYEIGSI
SKTFTAVILT YAINQGKIKL NDDIRKYLSG DYQNLQFEGT PIRIIDLCNH TSGLPGLPEN
FDSHSDYKEK NPYLNYSKEM INEYLSRFVV EELPVTRAEY SNLGFAILGM ILEDLYQLPL
EKLLQEVITF PLGMNNTTYE IPLTNHNLLT GYDHENGEEA GYWDLAAFKA AGGLKSDLED
MLVYLRANIN AYSKDFSFPH HQTDIQPGYG RGLAWVTQFF NDDTIIWHNG GTGGFRSYCG
FIKEKQTGLV VLSNSSKDVD DMAMEILLYS LQDQ
//
