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Database: UniProt
Entry: Q1D907_MYXXD
LinkDB: Q1D907_MYXXD
Original site: Q1D907_MYXXD 
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
//
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