ID Q1D907_MYXXD Unreviewed; 679 AA.
AC Q1D907;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 24-JAN-2024, entry version 105.
DE RecName: Full=Beta-lactamase {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
GN OrderedLocusNames=MXAN_2647 {ECO:0000313|EMBL:ABF90236.1};
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF90236.1, ECO:0000313|Proteomes:UP000002402};
RN [1] {ECO:0000313|EMBL:ABF90236.1, ECO:0000313|Proteomes:UP000002402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402};
RX PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA Kaplan H.B.;
RT "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
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|RuleBase:RU361140};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the class-D beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00007898, ECO:0000256|RuleBase:RU361140}.
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DR EMBL; CP000113; ABF90236.1; -; Genomic_DNA.
DR RefSeq; WP_011552717.1; NC_008095.1.
DR AlphaFoldDB; Q1D907; -.
DR STRING; 246197.MXAN_2647; -.
DR EnsemblBacteria; ABF90236; ABF90236; MXAN_2647.
DR GeneID; 41360023; -.
DR KEGG; mxa:MXAN_2647; -.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_009289_1_2_7; -.
DR OMA; SCDTYYY; -.
DR OrthoDB; 9766847at2; -.
DR Proteomes; UP000002402; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0017001; P:antibiotic catabolic process; IEA:InterPro.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR002137; Beta-lactam_class-D_AS.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR InterPro; IPR017790; Penicillin-binding_protein_2.
DR NCBIfam; TIGR03423; pbp2_mrdA; 1.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30627:SF2; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE MRDA; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
DR PROSITE; PS00337; BETA_LACTAMASE_D; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|RuleBase:RU361140};
KW Hydrolase {ECO:0000256|RuleBase:RU361140};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000002402};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 19..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 63..239
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 278..617
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 628..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..679
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 337
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR602137-50"
FT MOD_RES 340
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602137-50"
SQ SEQUENCE 679 AA; 74469 MW; 292AAFFFD26D52A0 CRC64;
MTPPTLGNTT PGRELKRRFL WLGLAMMAGL GLISIQLYRL QITRGEEYAA KSVANFVKEV
RLRADRGVIK DARGTILVDS RPSFDAFITP AFCTDCYEQV IPRLAELLQW DPDQRKKVED
MVRMGRRNAP FQPVPVRVDL SRDEYDRLAA RRDILDGVEV APVPHRHYRT NSVLSHVLGY
MNEITQEELE RLNGDGARYA LGDYIGRRGL ERYFEQRLRG TDGVRKEVVN ARGQTIEELN
DKLGDNAVVS PRPGNNLVLS IDMRLQEEAE RAFPGVTGAV VAIDANTGFI RALVSRPGFD
PNLLTGRVTP AQMALLSRDP LDPMINRVAA EHYSPGSTFK VVTALAAFKS GAFRPETVVN
CPGGYRLGAR TWRCHRDAGH GLVDGFTAMK SSCDTWYYKV ADTIGLDPIG EMGKALGLGS
PTGVNVVAEV PGIMPTSAYH DKASPGGYTK GMALNSSIGQ GDNNVTPLQL ALVYAAIANG
GTLYKPQMVN RLENLDGQTI ESFQPEVVRK VDLPPAHLKA VVDSLVMVAH EPGGTAYRAR
MNHMRDKDIL VASKTGTAQV ARLGAIRLRT HQMSYFERDH AWYAGFAPAD KPELVIVVLN
EHGGHGGSDA APTAMAVFQK YFDLKKLDAT APPPRPNQPY TPSSVTRAPS ADEAALTRRV
RPPARLPGDE EDRTRATAD
//