ID C2NH67_BACCE Unreviewed; 647 AA.
AC C2NH67;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 24-JAN-2024, entry version 46.
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 ORFNames=bcere0004_20300 {ECO:0000313|EMBL:EEK56626.1};
OS Bacillus cereus BGSC 6E1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=526970 {ECO:0000313|EMBL:EEK56626.1};
RN [1] {ECO:0000313|EMBL:EEK56626.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGSC 6E1 {ECO:0000313|EMBL:EEK56626.1};
RX PubMed=22645259; DOI=10.1101/gr.134437.111;
RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A.,
RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K.,
RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.;
RT "Genomic characterization of the Bacillus cereus sensu lato species:
RT Backdrop to the evolution of Bacillus anthracis.";
RL Genome Res. 22:1512-1524(2012).
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 -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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:EEK56626.1}.
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DR EMBL; ACLU01000050; EEK56626.1; -; Genomic_DNA.
DR AlphaFoldDB; C2NH67; -.
DR HOGENOM; CLU_009289_5_2_9; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000284; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046677; P:response to antibiotic; IEA:InterPro.
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; IPR007887; MecA_N.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR30627:SF25; PENICILLIN-BINDING PROTEIN 3; 1.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR Pfam; PF05223; MecA_N; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF54427; NTF2-like; 1.
DR SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136}.
FT DOMAIN 10..128
FT /note="NTF2-like N-terminal transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF05223"
FT DOMAIN 136..303
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 337..644
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 647 AA; 71251 MW; 2044EE28BCE06189 CRC64;
MLVGCGKEEK PQEAFDTYAK AWNKQKFAEM YDQLSEKAKK DISKKEFTEK YEKIYSGIEV
KNLKVEAGEV KEDKKDEGPI PFKVSMDTVG GKINFGHEAK MVKEKDGDKE SWKVDWTPDF
IFPGMTKDSK VRMQTTEPKR GEIYDRNGKG LATNGKASEI GLIPERLGDT APQTKETVAK
LLNMSVEEID QKLAAKWVKP GYLVPIGILP EGATQNTYID LPGVSTKPVN VRTYPLGEAA
AHLTGYIGKV NAEDLKTLQK KGYQADDPVG KAGLEQVLEE KLRGKKGGRV FVEDAQGKEI
KNLAKTDAVD GENVTLTIDS AVQEKTYNEM KGEAGSSAAI NPKSGETLAL VSSPAYDPNI
IARGTSKAQR EAWNNDPKKP MTNRFTQLSV PGSVFKPITA AIGLETKTID PKEELKIEGL
KWTKDSSWGN YYVTRVKDAN PIDFDKAMKY SDNIYFAQEA LKIGKDKFMS EAKKFGFDEK
LPIEYGFPAS KIANDGIKND IQMADTGYGQ GQVLMTPLHL ALTYAPIVND GNIPSPYIIK
TDKQPKVWKE NVISKGNQDI LKTAMTKVIN DPDGTGKIAK IDGMTLAGKT GTAELKVSKE
AEGKELGWFA AFDLNSPDMV ITMMIEDVKG RGGSNIPAEK VKHVFQK
//
