ID   A0A1I6BUS3_9BACI        Unreviewed;       697 AA.
AC   A0A1I6BUS3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
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=SAMN04488577_2458 {ECO:0000313|EMBL:SFQ84679.1};
OS   Bacillus sp. cl95.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1761761 {ECO:0000313|EMBL:SFQ84679.1, ECO:0000313|Proteomes:UP000199578};
RN   [1] {ECO:0000313|EMBL:SFQ84679.1, ECO:0000313|Proteomes:UP000199578}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL95 {ECO:0000313|EMBL:SFQ84679.1,
RC   ECO:0000313|Proteomes:UP000199578};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOYF01000003; SFQ84679.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6BUS3; -.
DR   STRING; 1761761.SAMN04488577_2458; -.
DR   OrthoDB; 9770103at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000199578; Unassembled WGS sequence.
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:0051301; P:cell division; IEA:UniProtKB-KW.
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   Cell cycle {ECO:0000313|EMBL:SFQ84679.1};
KW   Cell division {ECO:0000313|EMBL:SFQ84679.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199578}.
FT   DOMAIN          60..301
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          349..683
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   697 AA;  78560 MW;  E2E63E220B2F1758 CRC64;
     MNANPVKKKP HTPLRVNILF FCVFLLFSVL VVRLGVVQMV QGEDFAREVA RTEDIIVSYP
     VPRGKMYDRN GKVIVGNVSK NAITYTNYGV KQSEMLEIAK RLATLIEVKA DKVQERDKKD
     YWLLLNPEKA EAKISKAELK EWKKKLEGKK FDQKVYKIKL ERITETDLGE LTNQDLEIIA
     IYSIISSGYA LTPQIVKNEN VTDEEFAIVS ENLEYLPGVD TTTDWERSYH YDKTLKTVLG
     KVTDSSEGLP KEKLDYYVAR GYSLNERVGK SYIEMQYEDV LHGSKKKVKN ITDKGGKVIS
     TEVVSEGKSG NDLVLTIDMD LQLAVEKIIE EELLRVKQGG RTKLLDRSFV VLMDPRTGEV
     LTMAGKQIVR NKETGKMEIE DYALGTISSS YNVGSTVKGA TILTGLKTGV INTNTKFHDR
     PIKILDTPEK GSYSNRLGTL NPIGALRVSS NVYMFETAIR IGEGHYQYNQ PLPINKKAFD
     IIRDSFSQFG LGIRTGIDLP NEQIGFKGPS RLTGLLLDLS IGQYDTYTPM QLAQYVSTIA
     NDGYRVQPRI VKEIREPASA TNEIGRIVQD FKPNILNRIE LQEGWLETVQ EGFRQVMQTP
     GGTAYRRFGN ALYSPAGKTG TAQAFYDGPE RKNYKEPPPV MNLSLIGYAP FKNPEVAMSV
     MVPWAYEGES GHTANYEIGR RVMDAYFELK KQRMAQQ
//