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Database: UniProt
Entry: Q81BT5_BACCR
LinkDB: Q81BT5_BACCR
Original site: Q81BT5_BACCR 
ID   Q81BT5_BACCR            Unreviewed;       717 AA.
AC   Q81BT5;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   24-JAN-2024, entry version 100.
DE   RecName: Full=serine-type D-Ala-D-Ala carboxypeptidase {ECO:0000256|ARBA:ARBA00012448};
DE            EC=3.4.16.4 {ECO:0000256|ARBA:ARBA00012448};
GN   OrderedLocusNames=BC_3061 {ECO:0000313|EMBL:AAP10008.1};
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900 {ECO:0000313|EMBL:AAP10008.1, ECO:0000313|Proteomes:UP000001417};
RN   [1] {ECO:0000313|EMBL:AAP10008.1, ECO:0000313|Proteomes:UP000001417}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB
RC   9373 / NCTC 2599 / NRRL B-3711 {ECO:0000313|Proteomes:UP000001417};
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC         transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC         substituents of D-alanine.; EC=3.4.16.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034000};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the transpeptidase family.
CC       {ECO:0000256|ARBA:ARBA00007171}.
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DR   EMBL; AE016877; AAP10008.1; -; Genomic_DNA.
DR   RefSeq; NP_832807.1; NC_004722.1.
DR   RefSeq; WP_001249191.1; NZ_CP034551.1.
DR   AlphaFoldDB; Q81BT5; -.
DR   KEGG; bce:BC3061; -.
DR   PATRIC; fig|226900.8.peg.3136; -.
DR   HOGENOM; CLU_009289_7_0_9; -.
DR   OMA; TQYEMGS; -.
DR   OrthoDB; 9770103at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001417; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008658; F:penicillin binding; IBA:GO_Central.
DR   GO; GO:0071972; F:peptidoglycan L,D-transpeptidase activity; IBA:GO_Central.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IBA:GO_Central.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
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   Gene3D; 1.10.10.1230; Penicillin-binding protein, N-terminal non-catalytic domain, head sub-domain; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR005311; PBP_dimer.
DR   InterPro; IPR036138; PBP_dimer_sf.
DR   InterPro; IPR001460; PCN-bd_Tpept.
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.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001417};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          65..312
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          357..692
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   COILED          152..186
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   717 AA;  81498 MW;  63B3C3D64CA92581 CRC64;
     MRQKKEQKKQ SKKKKTHIPF RLNVLFFIVF LLFSAIIIQL GKVQIIDGET YRNEVNKKED
     VTVSTPVPRG KMFDRQGHVI VNNKPLRTVT YTKMRGVDSK EVLQVARDLA KLIEMSQEDM
     DKLTETDKKD FWMQLNEKRA AAKVTKEDES KFRKQEIEGK ELDKKVEELR RERITQEELN
     ELSKEDIEVL VIKSKMNAGY KMTPQIVKKD VSQNEYAVVS ERLASLPGVD TTVDWEREYP
     NDKILRSILG SVSNENEGLP REQLDYYLVR DYNRNDRIGK SYIEKQYEDA LHGTKEQSKN
     IMDKAGKIVR TEKVTEGKSG NNLMLTVDMD LQKRVEGSLE KNLRAFHAAE PMMDRAFVVM
     MNPKNGQILS MAGKKIVNKD GGMQIEDYAL GTMTSSYELG STVKGATLLT GYQTEAIKPY
     THFFDAPMYF KGSSKPKKSW KEFGDIDDLR ALQVSSNVYM FNTALKMAGI NYVPNNPLDI
     KQETFNKMRY YFRQFGLGVS TGIDLPNESI GQVGRTDNIP GFLLDYAIGQ YDTYTPLQLA
     QYISTIANGG YRMKPQIVQE VREQPNRPED VGKVVRSIEP VVLNRVDMDT SYINHVKEGF
     RRVFQEADGT GTGTFKGLPY KPAGKTGTAE TVYGGESDIG RDENNNRKKC YNLTLAGYAP
     YDADPEVAFS VVVPWVNDDK SGINSAIGKE ILDAYFELKT NRSNANSIPV EQPNKAQ
//
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