ID A0A3S0LHV4_9BACI Unreviewed; 651 AA.
AC A0A3S0LHV4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=EKG37_04310 {ECO:0000313|EMBL:RTR35858.1};
OS Bacillus yapensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2492960 {ECO:0000313|EMBL:RTR35858.1, ECO:0000313|Proteomes:UP000271374};
RN [1] {ECO:0000313|EMBL:RTR35858.1, ECO:0000313|Proteomes:UP000271374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XXST-01 {ECO:0000313|EMBL:RTR35858.1,
RC ECO:0000313|Proteomes:UP000271374};
RA Yu L., Xu X., Tang X.;
RT "Bacillus yapensis draft genome sequence.";
RL Submitted (DEC-2018) 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}.
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:RTR35858.1}.
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DR EMBL; RXNT01000002; RTR35858.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S0LHV4; -.
DR OrthoDB; 9770103at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000271374; 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:UP000271374};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 58..285
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 327..644
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 651 AA; 73157 MW; 25F12319E9E490ED CRC64;
MKGQKKNKSL SIRLNILFLI AFLLFFILIL RLGFIQIVKG EEYKSESEKT TTTVYAWDAP
RGKIYDRNRN VLVDNEAVNT LTYKNVNGDS QNEKLELAKK LAELIEVDTE RVTERDKKDF
YILTRKEKAY GKLTEKEKKE LDDDGEYKLI LERITDKDLS ALSDDEMEIL AIKREMDIDS
ASENRIKSGL TLEEMAKVNE RLGELPGINI KLDSKRKYVN GDTLRQIFGN VGQIPEEEAK
SYKKDGYELS DLVGTSFLEQ QYEKWLRGKK EKQTYVEGPT GEITDVKITP GETGKDLVLT
IDLDFQQKVD KILEEELKSE SQAESAYAVV TNPTTGEILA ISGKKKSGTK IVDETYGTIY
NSYAMGSAVK GATVLTGYET GVISPGDTFV DEPIKISGTP IKKSYSNMGR INDLTALERS
SNVYMFNIAM KIGEYDYAKR SGFRNPEKAY ETMRKYFSQF GLGIETEIDL PKEAIGYNGG
VQKLGNLMDF VIGQFDTYTP LQLAQYVSTI ANDGKRVQPH FMKEVSEPNH VSGSPGEVIE
EFEPNILNEV DMDLSYIERV QEGFRLVMNG SRGTATSYFK GVTYDPVGKT GTAQVSDGNG
GYNYNLTLVG YAPYENPEIA ISVVVPDVET DGSSINKYIG KRILDTYFEK K
//
