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Database: UniProt
Entry: A0A286DXV4_9ACTN
LinkDB: A0A286DXV4_9ACTN
Original site: A0A286DXV4_9ACTN 
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
//
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