(data stored in ACNUC7421 zone)

SWISSPROT: C1AR67_RHOOB

ID   C1AR67_RHOOB            Unreviewed;       317 AA.
AC   C1AR67;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 54.
DE   RecName: Full=Beta-lactamase {ECO:0000256|RuleBase:RU361140, ECO:0000256|SAAS:SAAS00129357};
DE            EC=3.5.2.6 {ECO:0000256|RuleBase:RU361140, ECO:0000256|SAAS:SAAS00129357};
GN   OrderedLocusNames=ROP_02970 {ECO:0000313|EMBL:BAH48544.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH48544.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH48544.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH48544.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: A beta-lactam + H(2)O = a substituted beta-
CC       amino acid. {ECO:0000256|RuleBase:RU361140,
CC       ECO:0000256|SAAS:SAAS00129358}.
CC   -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC       {ECO:0000256|RuleBase:RU361140, ECO:0000256|SAAS:SAAS00559532}.
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DR   EMBL; AP011115; BAH48544.1; -; Genomic_DNA.
DR   RefSeq; WP_012687551.1; NC_012522.1.
DR   ProteinModelPortal; C1AR67; -.
DR   STRING; 632772.ROP_02970; -.
DR   MEROPS; S11.A01; -.
DR   EnsemblBacteria; BAH48544; BAH48544; ROP_02970.
DR   KEGG; rop:ROP_02970; -.
DR   PATRIC; fig|632772.20.peg.338; -.
DR   eggNOG; ENOG4108J4B; Bacteria.
DR   eggNOG; COG2367; LUCA.
DR   HOGENOM; HOG000201073; -.
DR   KO; K17836; -.
DR   OMA; FKTLACA; -.
DR   OrthoDB; POG091H023N; -.
DR   BioCyc; ROPA632772:GH0Q-296-MONOMER; -.
DR   Proteomes; UP000002212; Chromosome.
DR   GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-UniRule.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR000871; Beta-lactam_class-A.
DR   InterPro; IPR023650; Beta-lactam_class-A_AS.
DR   PRINTS; PR00118; BLACTAMASEA.
DR   SUPFAM; SSF56601; SSF56601; 1.
DR   PROSITE; PS00146; BETA_LACTAMASE_A; 1.
PE   3: Inferred from homology;
DR   PRODOM; C1AR67.
DR   SWISS-2DPAGE; C1AR67.
KW   Antibiotic resistance {ECO:0000256|RuleBase:RU361140,
KW   ECO:0000256|SAAS:SAAS00063120};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002212};
KW   Hydrolase {ECO:0000256|RuleBase:RU361140,
KW   ECO:0000256|SAAS:SAAS00483625, ECO:0000313|EMBL:BAH48544.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     36       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        37    317       Beta-lactamase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5002904722.
SQ   SEQUENCE   317 AA;  32964 MW;  59E7892EFB1EF4E3 CRC64;
     MLTHRNHPKP RRTGRRGVVA LALALPLLAG ACTATAEQTL PATSESTAPD HESLDAKIEA
     LEAQYATRIG VTAVDPQTGA VYSHRGDERF AMCSTFKAYA SAAVLRKIED GSTSLDKTVM
     IEPADLVENS PVTAAAVGTP MTLGQIAEAA LTQSDNTAGN YLLREIGGPQ AITALARDVG
     DASTRLDRWE TELNTAFRGD PRDTTTPTGL AHGFRALLLG DALDAASRGQ LLDWMRASKT
     SDKRMRAGLP PGWTAADKTG GGGFGTANDA GVAWSPDGSP IVLAVLTDSL TNQEDAQGNS
     QAIADTTTAV IAGLTAP
//

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