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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//