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Database: UniProt
Entry: Q2JKE0_SYNJB
LinkDB: Q2JKE0_SYNJB
Original site: Q2JKE0_SYNJB 
ID   Q2JKE0_SYNJB            Unreviewed;       426 AA.
AC   Q2JKE0;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   SubName: Full=Carboxylesterase, beta-lactamase family {ECO:0000313|EMBL:ABD02849.1};
GN   OrderedLocusNames=CYB_1894 {ECO:0000313|EMBL:ABD02849.1};
OS   Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium
OS   Yellowstone B-Prime).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=321332 {ECO:0000313|EMBL:ABD02849.1, ECO:0000313|Proteomes:UP000001938};
RN   [1] {ECO:0000313|EMBL:ABD02849.1, ECO:0000313|Proteomes:UP000001938}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA-2-3B'a(2-13) {ECO:0000313|Proteomes:UP000001938};
RX   PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA   Bhaya D., Grossman A.R., Steunou A.S., Khuri N., Cohan F.M., Hamamura N.,
RA   Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT   "Population level functional diversity in a microbial community revealed by
RT   comparative genomic and metagenomic analyses.";
RL   ISME J. 1:703-713(2007).
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DR   EMBL; CP000240; ABD02849.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2JKE0; -.
DR   STRING; 321332.CYB_1894; -.
DR   MEROPS; S11.A01; -.
DR   KEGG; cyb:CYB_1894; -.
DR   eggNOG; COG2367; Bacteria.
DR   HOGENOM; CLU_031960_1_0_3; -.
DR   OrthoDB; 9775096at2; -.
DR   Proteomes; UP000001938; 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:InterPro.
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:SF4; SLR0121 PROTEIN; 1.
DR   Pfam; PF13354; Beta-lactamase2; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001938};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        100..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          175..384
FT                   /note="Beta-lactamase class A catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF13354"
FT   REGION          1..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          126..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..142
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   426 AA;  46607 MW;  D79ECC401A5D02C7 CRC64;
     MTRARERKGT DPSALAGRRP LPEKSRDPRR PPQPAKNAVP PPEGSKPQTG SGRLLPAPRG
     SLLVSRPQPL RLARQKAIAR LRQRAARPRR LRRSPSLGQV LLRGLSLSLI LGLTMAGLSQ
     LLQSTTAGRT EQSTTQLGDP PPSAFPSNIL PGEAIPALQE RLAALADQPG LTAGALFWEV
     ETGAFAGVRP DQAFPAASVI KIPILLAFFQ AVETGQVRLD EQLTLREDLK GGGAGVLQTR
     PLGSQVSALE AATLMITLSD NFATNLIIDR LGGQETLNQK FRQWGLQHTQ ISWWLPDLEG
     TNTSSPRDMV WLLSQVEQGR MLNRRSRDRF LDILWRTQRL SYFRPNLGQE VRIAHKTGTL
     GSVVGDAGIL DLPNGRRYVA AVWVKRETPN DPRAEGLIAS LSQAAYEFWS APEDPTAKDS
     MGSLER
//
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