(data stored in ACNUC7421 zone)

SWISSPROT: B1VQI5_STRGG

ID   B1VQI5_STRGG            Unreviewed;       312 AA.
AC   B1VQI5;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   07-JUN-2017, entry version 63.
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=SGR_457 {ECO:0000313|EMBL:BAG17286.1};
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=455632 {ECO:0000313|EMBL:BAG17286.1, ECO:0000313|Proteomes:UP000001685};
RN   [1] {ECO:0000313|EMBL:BAG17286.1, ECO:0000313|Proteomes:UP000001685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4626 / NBRC 13350 {ECO:0000313|Proteomes:UP000001685};
RX   PubMed=18375553; DOI=10.1128/JB.00204-08;
RA   Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA   Yamashita A., Hattori M., Horinouchi S.;
RT   "Genome sequence of the streptomycin-producing microorganism
RT   Streptomyces griseus IFO 13350.";
RL   J. Bacteriol. 190:4050-4060(2008).
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; AP009493; BAG17286.1; -; Genomic_DNA.
DR   RefSeq; WP_012377810.1; NC_010572.1.
DR   ProteinModelPortal; B1VQI5; -.
DR   STRING; 455632.SGR_457; -.
DR   MEROPS; S11.A01; -.
DR   EnsemblBacteria; BAG17286; BAG17286; SGR_457.
DR   GeneID; 6211944; -.
DR   KEGG; sgr:SGR_457; -.
DR   PATRIC; fig|455632.4.peg.434; -.
DR   eggNOG; ENOG4108J4B; Bacteria.
DR   eggNOG; COG2367; LUCA.
DR   HOGENOM; HOG000201073; -.
DR   KO; K17836; -.
DR   OMA; EWMKGNA; -.
DR   Proteomes; UP000001685; 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   InterPro; IPR006311; TAT_signal.
DR   PRINTS; PR00118; BLACTAMASEA.
DR   SUPFAM; SSF56601; SSF56601; 1.
DR   PROSITE; PS00146; BETA_LACTAMASE_A; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
DR   PRODOM; B1VQI5.
DR   SWISS-2DPAGE; B1VQI5.
KW   Antibiotic resistance {ECO:0000256|RuleBase:RU361140,
KW   ECO:0000256|SAAS:SAAS00063120};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001685};
KW   Hydrolase {ECO:0000256|RuleBase:RU361140,
KW   ECO:0000256|SAAS:SAAS00483625};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001685};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     30       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        31    312       Beta-lactamase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5002769955.
SQ   SEQUENCE   312 AA;  32605 MW;  F3F1C5116FB339F2 CRC64;
     MSRLPNPHAR RSVLRLLGGA LLSAPLTACG TESDAPAPSP AGKPAGTPPA RADGRAFEAL
     EKEYAARLGV YAVDTGTGTT VAHRDGERFA YASTFKALAA GAVLRRYGLG GLERIVTYRR
     EDLVDHSPVT EKHVATGMSL GALCDAAVRF SDNTAGNLLF DAVGGPRKLQ AVLAGLGDEV
     TRMVRRETEL NEWTPGATRD TSTPRALAED LRAFVLGDAL GGPERARLTQ WLTTNTTGGE
     LIRAGVPKGW TVGDKTGAGS TYGTRNDIAV VWPPDAAPLV LAVLSNRTAA DADHDNTLIA
     KAASAAVTAL TR
//

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