ID K9W5P1_9CYAN Unreviewed; 481 AA.
AC K9W5P1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN ORFNames=Cri9333_3988 {ECO:0000313|EMBL:AFZ14795.1};
OS Crinalium epipsammum PCC 9333.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Gomontiellaceae;
OC Crinalium.
OX NCBI_TaxID=1173022 {ECO:0000313|EMBL:AFZ14795.1, ECO:0000313|Proteomes:UP000010472};
RN [1] {ECO:0000313|EMBL:AFZ14795.1, ECO:0000313|Proteomes:UP000010472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 9333 {ECO:0000313|EMBL:AFZ14795.1,
RC ECO:0000313|Proteomes:UP000010472};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Crinalium epipsammum PCC 9333.";
RL Submitted (JUN-2012) 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|ARBA:ARBA00001526};
CC -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00009009}.
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DR EMBL; CP003620; AFZ14795.1; -; Genomic_DNA.
DR RefSeq; WP_015204895.1; NC_019753.1.
DR AlphaFoldDB; K9W5P1; -.
DR STRING; 1173022.Cri9333_3988; -.
DR KEGG; cep:Cri9333_3988; -.
DR PATRIC; fig|1173022.3.peg.4306; -.
DR eggNOG; COG2367; Bacteria.
DR HOGENOM; CLU_045682_0_0_3; -.
DR OrthoDB; 440093at2; -.
DR Proteomes; UP000010472; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:InterPro.
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; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR045155; Beta-lactam_cat.
DR InterPro; IPR000871; Beta-lactam_class-A.
DR PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13354; Beta-lactamase2; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000010472};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 94..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 208..449
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
FT REGION 51..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 9..50
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 481 AA; 54022 MW; 1A59F21C9F95F07B CRC64;
MSYKSEVKLD QRDQEIAALE KELNLADQLI KKLKRQNTVL KHRINFLENN SRPHPALVAS
RGNSPRPNKR EYPPGKGGAL VRQQRSKTRA IKLWRLRVAT IAIALLGFTL VNWAVSSLTK
LKPNENPKSV AAKLASASLS GQQSTIPAWA KASSQDIPTR QSGKEDLEIV YNLTTPPQFQ
PSEKLQVIVD ELVAIADSKK LPTKDLSITL IDAKTGEIAG YQQKELRYPA SVVKMFWMVA
LYGQLENGIW KNPQDFNLYT SKMIEHSNND ASSFILDHIT NTKSQDKLPD NQFTVWLNQR
DSVNRFFSSA GYEGININQK TYPIYYLRME EPAGTESQMR GDPERPLRNV ITTDHSARLL
YEICLTKQAI SAVASEKMCG LLKRDLKPEA WKTNSETSED FNPIVGFSGQ SLRDSEVNFY
SKAGLTSSTR QEAAFVATKD NSTAYVIAIA GGDRAYSSDY KLFPKMSSVV FEKMVERSAR
K
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