ID B7IXA8_BACC2 Unreviewed; 586 AA.
AC B7IXA8;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
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=BCG9842_B2822 {ECO:0000313|EMBL:ACK97187.1};
OS Bacillus cereus (strain G9842).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405531 {ECO:0000313|EMBL:ACK97187.1, ECO:0000313|Proteomes:UP000006744};
RN [1] {ECO:0000313|EMBL:ACK97187.1, ECO:0000313|Proteomes:UP000006744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G9842 {ECO:0000313|EMBL:ACK97187.1,
RC ECO:0000313|Proteomes:UP000006744};
RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA Ravel J., Sutton G.;
RT "Genome sequence of Bacillus cereus G9842.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001186; ACK97187.1; -; Genomic_DNA.
DR RefSeq; WP_000902383.1; NC_011772.1.
DR AlphaFoldDB; B7IXA8; -.
DR KEGG; bcg:BCG9842_B2822; -.
DR HOGENOM; CLU_009289_8_1_9; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000006744; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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 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; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 37..197
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 241..567
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 586 AA; 65676 MW; A9DCF7557224F5A3 CRC64;
MLHIKRWRFF AVFSIVGLIL LILLKINFIS ITIATSSAER GKIFDQNGVI LATNKKVKSL
YCTSNDEKLS KQDTSNTLAF FNQFSSEFQH DISTENIKSQ LQQSCKKQTM NDIPLYSDIT
ENELAFINKN KPNNVIIKNE WIRYYPKHEI GSQVIGYVEN DLNSKHKAVG KSGIELQYEN
DLKGKPGKTL IFKLNNKKFL WNIQTVQKGK DVRLALDSEL QQKAEEALRS QIKKTPDAKA
GYAVVSDAKT GAILTMANTA VFDPNILNTR ISSRKENINS LSQNKAIQKL KYGESYVNMA
STIKPLTILI GLNEKLFQPE DTYLDKGTFQ YDNQNNITNA PGTPTGEITP RQAIINSSNT
FMTAKVALPL FNQNNGNIEK VAHIWTDYLI QFGLRSKTGI DLPFEEDGQY EFHPSNKFEN
GISALLNASW GGNEVHTPLQ LAQYAATLAS KGDKYKPQTV SAIISPDGKE TKKFKPILES
SNRYPMNFWS VVQGGMSQNI EEIKKLPFDV AGKTGITGFP NEQERMINHS LFIAYAPTED
PQIAVSVVIP GSNSEKNIAA LVTSEILESW HTLQKENKNK EEGSLK
//
