ID T2JS57_CROWT Unreviewed; 410 AA.
AC T2JS57;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Beta-lactamase {ECO:0000313|EMBL:CCQ68060.1};
DE EC=3.5.2.6 {ECO:0000313|EMBL:CCQ68060.1};
GN ORFNames=CWATWH0402_4762 {ECO:0000313|EMBL:CCQ68060.1};
OS Crocosphaera watsonii WH 0402.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Crocosphaera.
OX NCBI_TaxID=1284629 {ECO:0000313|EMBL:CCQ68060.1, ECO:0000313|Proteomes:UP000018130};
RN [1] {ECO:0000313|EMBL:CCQ68060.1, ECO:0000313|Proteomes:UP000018130}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH 0402 {ECO:0000313|EMBL:CCQ68060.1,
RC ECO:0000313|Proteomes:UP000018130};
RA Bench S.;
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCQ68060.1, ECO:0000313|Proteomes:UP000018130}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH 0402 {ECO:0000313|EMBL:CCQ68060.1,
RC ECO:0000313|Proteomes:UP000018130};
RA Bench S.R., Heller P., Frank I., Arciniega M., Shilova I.N., Zehr J.P.;
RT "Whole genome comparison of six Crocosphaera watsonii strains with
RT differing phenotypes.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCQ68060.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CAQN01000692; CCQ68060.1; -; Genomic_DNA.
DR AlphaFoldDB; T2JS57; -.
DR Proteomes; UP000018130; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC.
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 Hydrolase {ECO:0000313|EMBL:CCQ68060.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 45..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 143..351
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 410 AA; 45679 MW; 12A01054763EF08E CRC64;
MNNNQKQARI VSGKGKNSKK QLSREKTVSQ PKKPRPYPSK RSPNLLIQCF LYVLRIGVMG
VGIGAIAGTT LTIINPQDIL AAYTKASQLI KPSPEENKEN KEEKPEKLTP KTSASVPVSK
ELTALQEKIQ KIDAKYPNVK PQAWFIDLDN GAYVTYNGTQ PIPAASTIKI PVLVAFFEEV
DKGNIHLDQM LTMTKDVMVS GSGDMQYMGI NKKFTALEVA RKMIVISDNT ATEMLVKQMG
GKEVLNKRFK EWGMKNTEIN NILPDLEGTN KTSSEDLSKL LARIERGDLI SARSRDRLID
IMEGTRTRTL LPQGLEKQAN IAHKTGDIGT IIGDAGIIDM PTGKRYIGAV FAERAYNDVA
GRHLIQDISR TVYQHFKHYQ PRPVPKPITK QVESQPQPEE KPAENNQTET
//
