ID F2C9Z2_STRSA Unreviewed; 427 AA.
AC F2C9Z2;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, 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};
GN ORFNames=HMPREF9386_1998 {ECO:0000313|EMBL:EGF13222.1};
OS Streptococcus sanguinis SK330.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=888813 {ECO:0000313|EMBL:EGF13222.1, ECO:0000313|Proteomes:UP000005955};
RN [1] {ECO:0000313|EMBL:EGF13222.1, ECO:0000313|Proteomes:UP000005955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK330 {ECO:0000313|EMBL:EGF13222.1,
RC ECO:0000313|Proteomes:UP000005955};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (FEB-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}.
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:EGF13222.1}.
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DR EMBL; AFBD01000008; EGF13222.1; -; Genomic_DNA.
DR RefSeq; WP_002916257.1; NZ_GL878550.1.
DR AlphaFoldDB; F2C9Z2; -.
DR PATRIC; fig|888813.3.peg.1967; -.
DR HOGENOM; CLU_053694_0_0_9; -.
DR Proteomes; UP000005955; Unassembled WGS sequence.
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: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 Hydrolase {ECO:0000313|EMBL:EGF13222.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..427
FT /note="beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003276377"
FT DOMAIN 206..407
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 427 AA; 48470 MW; F1D4C86CFA475007 CRC64;
MRKFLLLIFL LPALFSSITV ISTEKDFVLD EEEKYHFTST AYGRYYDSIP TNPNVYEETP
TFTDSTLSKT AGKLVPDQPI QITGFYVNEE GVPIFKLKNG QFVIADKNTI YEDTVQSIQD
IHQEMWLKPG FTLYDKANIN GAKKINTTVA PYTKVNIVQI VQTVKGTYAQ VEGQGWVSME
FLDETDNRMD KVQEILSSKY NKADYSIYVK QLDTGKEAGI NQDQEMYSAS VTKLPYLYYV
QEQLDQKKLS LDQKFKYIGA VNDFTGAYEP EGSGSIAKSA DDKEYSVQDL INRVAKESDN
VSHNILGYYA TNQSDKNFQQ TINKIAGKKW DVEERQASSR MTGNILEAIY EQNGMIIDAL
SQTNYDNQRI SKNIDVKVAH KIGDAYDFKH DAAIVYTDSP FIIVIFTNNS NYDNISQIAD
DVYGVLK
//
