ID   A0A1G8CV25_9BACI        Unreviewed;       670 AA.
AC   A0A1G8CV25;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
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=SAMN05192534_10694 {ECO:0000313|EMBL:SDH49351.1};
OS   Alteribacillus persepolensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alteribacillus.
OX   NCBI_TaxID=568899 {ECO:0000313|EMBL:SDH49351.1, ECO:0000313|Proteomes:UP000199163};
RN   [1] {ECO:0000313|EMBL:SDH49351.1, ECO:0000313|Proteomes:UP000199163}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21632 {ECO:0000313|EMBL:SDH49351.1,
RC   ECO:0000313|Proteomes:UP000199163};
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; FNDK01000006; SDH49351.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8CV25; -.
DR   STRING; 568899.SAMN05192534_10694; -.
DR   OrthoDB; 9770103at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000199163; 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: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   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199163};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          61..281
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          331..647
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   670 AA;  75307 MW;  4F69941A3DE701B1 CRC64;
     MKKKKNGTTE KNGIPFRLNV LFFAVFILFS ALILRLGFIQ IVQGDEFERE QEQTSSEAVR
     IDAPRGLMYD RNGELVVDNE LVLTLTYTNE QSVSDEERIR IATELSEIIE VDDDDIENIP
     ERDLKDYWLV THPDEALSLI TQEDRDSVEE DEELYQIQLD RISDEQLQEL DPQREIIAIW
     REMTSGYYDS PQRIKKGLAQ EEAHRISERL DDLPGVDILR DANRNYLYED AFPRFFGRIG
     SIPRESVDQY LAKGYDRSDE VGTSFLEQYY EEALRGQKGE VSNDSREESS GSRGHDLVLS
     VDMALQQEVE TIIDNEVDSA AGSFINDKSA YVVMMEPDTG ELLAVAGYSD QIGTIASSFE
     MGSTVKPATV LLGLETGVIS EHTVVYDRTI NLPSTPPISS VSALGPVNYL SALERSSNVY
     MAHIAMEMAG YQYGVSQTWN VAQYNKAYDT FRYYYEQFGL GVETGIDLPY ETTGINGGNQ
     SPGNLLYLSF GQFDTYTPMQ LAQYTAAIAN DGYRMKPQLV KQIREPNADK SELGAVRQQF
     EPTVLNKVDI DERYIHMAQQ GMWRVVNGSR GTARSYFNNT DYVAAGKTGT AEITVRREGT
     DNYVDGNNQA FIGYAPYDDP EVAIAVIVPN VYVSGTSGIA NRIARSSLDA YFDLKEERPD
     IEPAGEETSE
//