ID A0A286DXV4_9ACTN Unreviewed; 977 AA.
AC A0A286DXV4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:SOD63507.1};
GN ORFNames=SAMN06297387_11154 {ECO:0000313|EMBL:SOD63507.1};
OS Streptomyces zhaozhouensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1300267 {ECO:0000313|EMBL:SOD63507.1, ECO:0000313|Proteomes:UP000219072};
RN [1] {ECO:0000313|EMBL:SOD63507.1, ECO:0000313|Proteomes:UP000219072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.7095 {ECO:0000313|EMBL:SOD63507.1,
RC ECO:0000313|Proteomes:UP000219072};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S11 family.
CC {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
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DR EMBL; OCNE01000011; SOD63507.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A286DXV4; -.
DR OrthoDB; 3530815at2; -.
DR Proteomes; UP000219072; Unassembled WGS sequence.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR018044; Peptidase_S11.
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; PF00768; Peptidase_S11; 1.
DR PRINTS; PR00725; DADACBPTASE1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:SOD63507.1};
KW 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:0000313|EMBL:SOD63507.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000219072};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 645..837
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT REGION 1..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..305
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..383
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..440
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..543
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 653
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 656
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 719
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 819
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 977 AA; 98971 MW; EFC966863596CD36 CRC64;
MSGESPDRSV RDRERESSEK TSEDPGRVPQ DAKVPGDEGR KAAAEGAARD DAQGGDGGTG
IAGRRDAEPG EAADADADGR SERNEGEGDD ADAGAQGEDG AGAVEGVKAD APSDATTMLR
LPASGSSAPA DAERRAEEAA EAEGANASGD PVEGGTAEGR SGDDDGGESP SGDDAANEPG
GGTAASGAGD RLTADLRLPA DARDKGTTEL RSPSADEAAS PKAGDKGTTE LRSPASGDAA
PTGGQARGVS GAGSGSGSVA GSGDKGTTEL RPSEKGREGV EASDGGADGE PDAEADGAEA
DGAEADGAEA GDHATRMLRL PASEKETGDR LTTELRAPSE EADSSRQTDE IDEGDKGDKG
DEGTTQLRLP AEEKSDTEEK SGTEGGSDAT AMLRLPATGK GPDGGAEGDA GEDDAPEDGK
AAKGSKGSKD NKDNKESRGG AGDGGRNGGK PDVTAAMPVL GEKDEALAAP PRPSAPPKGA
EGTKGTEGAK ESKESKGGED RASDSRAAEP ASPAKPDPTP SAPPEPEAAP PAPVLPPKPE
AAPPPADADR DPLELLAALT NKPAPPPTPL RTLVRRVKIW TPLAVLALIL LVVAQVLRPL
PEPGLELTAS ETYTFEGELG SVPWPEQGQA QLDVQGLGSF GSSGEQEPVP IASVAKVMTA
YVILRDHPMD PETDGASIPV DQQAEDEVEL IAENESIVEV TAGQELTQRE AIQAIMIASA
NNVARLLARW DAGSEEAFVE KMNEAAEELG MTDTTYTDPS GLRPETVSTA ADQTKLGREV
MKDPFFREVV RMPSYVDSEG KEQLNWNHLV PLDGVVGIKT GTTTTAGGNL LFAAEQQVGD
NTQLIVGAVL AQPPHPSDNS ILTGALTAGK ELIDFGQEQL VAEPMLAAGD VVGEVDDGLG
GGVPLVITED LPVVGWPGLD VGLELVENAD GVPGSGEAGT VVGTLRAGDG EGAVEVPVAL
GEALSEPSFG ARLTRIT
//