ID H8YZK4_9GAMM Unreviewed; 328 AA.
AC H8YZK4;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
DE AltName: Full=Penicillinase {ECO:0000256|ARBA:ARBA00030171};
GN ORFNames=Thi970DRAFT_02379 {ECO:0000313|EMBL:EIC22131.1};
OS Thiorhodovibrio frisius.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiorhodovibrio.
OX NCBI_TaxID=631362 {ECO:0000313|EMBL:EIC22131.1, ECO:0000313|Proteomes:UP000002964};
RN [1] {ECO:0000313|Proteomes:UP000002964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=970 {ECO:0000313|Proteomes:UP000002964};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Overmann J.,
RA Frigaard N.-U., Bryant D.A., Woyke T.J.;
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EIC22131.1, ECO:0000313|Proteomes:UP000002964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=970 {ECO:0000313|EMBL:EIC22131.1,
RC ECO:0000313|Proteomes:UP000002964};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Zhang X., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K., Liu Z.,
RA Overmann J., Frigaard N.-U., Bryant D., Woyke T.;
RL Submitted (NOV-2011) 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; JH603169; EIC22131.1; -; Genomic_DNA.
DR RefSeq; WP_009148716.1; NZ_JH603169.1.
DR AlphaFoldDB; H8YZK4; -.
DR STRING; 631362.Thi970DRAFT_02379; -.
DR eggNOG; COG2367; Bacteria.
DR HOGENOM; CLU_962031_0_0_6; -.
DR OrthoDB; 7054239at2; -.
DR Proteomes; UP000002964; Unassembled WGS sequence.
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 InterPro; IPR006311; TAT_signal.
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.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW Reference proteome {ECO:0000313|Proteomes:UP000002964}.
FT DOMAIN 138..275
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 328 AA; 36396 MW; DB8833CE9E88CE69 CRC64;
MNKLFLPSSI QNNTVETAPD APPGGVDASA HLSRRAFLGN LTLATGGLLL GGLPDVLAAA
PGSLQAQVSA LVNRMRAEGR ISSNERTSWS IYDFSSRQKL VAINEDIPRQ AASMIKPFVA
QAFFYTTERR GSGLKYTSSV RDIMEQSIRR SSNSATNELM HMVSRGNGNH GPGDVETVLK
RQAPGVFRET SIVEYIPAGG RTYRNQASAH DYSRFLFALW HSRLPQAQEL REIMGLPNHD
RITRRVSSIP ANVRVYDKTG STARLCGNMG IIECRDSRGR PMPYTFIGII ERDSRTESYT
SWISARSNAI RSVSNLVYLY MKDRHQLV
//
