ID A6BJG3_9FIRM Unreviewed; 452 AA.
AC A6BJG3;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 24-JAN-2024, entry version 64.
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=DORLON_02458 {ECO:0000313|EMBL:EDM62208.1};
OS Dorea longicatena DSM 13814.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Dorea.
OX NCBI_TaxID=411462 {ECO:0000313|EMBL:EDM62208.1, ECO:0000313|Proteomes:UP000004016};
RN [1] {ECO:0000313|EMBL:EDM62208.1, ECO:0000313|Proteomes:UP000004016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13814 {ECO:0000313|EMBL:EDM62208.1,
RC ECO:0000313|Proteomes:UP000004016};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDM62208.1, ECO:0000313|Proteomes:UP000004016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13814 {ECO:0000313|EMBL:EDM62208.1,
RC ECO:0000313|Proteomes:UP000004016};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Dorea longicatena (DSM 13814).";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Removes C-terminal D-alanyl residues from sugar-peptide cell
CC wall precursors. {ECO:0000256|ARBA:ARBA00003217}.
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 peptidase S11 family.
CC {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
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:EDM62208.1}.
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DR EMBL; AAXB02000016; EDM62208.1; -; Genomic_DNA.
DR RefSeq; WP_006427620.1; NZ_DS264402.1.
DR AlphaFoldDB; A6BJG3; -.
DR eggNOG; COG1686; Bacteria.
DR HOGENOM; CLU_027070_7_0_9; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000004016; Unassembled WGS sequence.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 2.60.410.10; D-Ala-D-Ala carboxypeptidase, C-terminal domain; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR015956; Peniciliin-bd_prot_C_sf.
DR InterPro; IPR018044; Peptidase_S11.
DR InterPro; IPR012907; Peptidase_S11_C.
DR InterPro; IPR037167; Peptidase_S11_C_sf.
DR InterPro; IPR001967; Peptidase_S11_N.
DR PANTHER; PTHR21581; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR21581:SF32; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACB; 1.
DR Pfam; PF07943; PBP5_C; 1.
DR Pfam; PF00768; Peptidase_S11; 1.
DR PRINTS; PR00725; DADACBPTASE1.
DR SMART; SM00936; PBP5_C; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF69189; Penicillin-binding protein associated domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000313|EMBL:EDM62208.1}; Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 337..436
FT /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00936"
FT REGION 44..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 112
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 115
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 169
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 284
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 452 AA; 51011 MW; C59290F87BFB8963 CRC64;
MKRRPHKIVS VVLLAVLIAG MGMACRIQSL ESRNKRWTEN TETAGKILTE SGKKEAQKQT
NGTENDDAAQ NAKRVFGDEP AELYARSAVL MDADSGRVLF GKDTDVVRPM ASTTKIMTCI
LALESLREHP DQTIEVSDQA ASQPKVHLGM QKGEVFYIKD LLYSLMLESH NDSAVAVAEG
IAGSVEEFAK EMNAKAAEIG CKNTHFITPN GLDAEDEGGV HSTTAEDLAK IMRYCIMTSG
EKETFLEVTR TKEYQFQDAD RKRTFSCHNH NAFLDMMDGA LSGKTGFTAD AGYCYVGSLR
WDDRTFIVAL LACGWPNNKG YKWKDTRKLM EYGLEHYQYR DIDKKMQIPE IKVAGGVDDK
KPYQYCLNVP VKIERPAEEN SKILMRDGEE LRAKLELAKY WNAPLKKGEK IGMLTYYLDG
YKVAEYELKN EKTVAKRDFS WCIFWIIKSV ML
//
