GenomeNet

Database: UniProt
Entry: A0A089YSN4_STRGA
LinkDB: A0A089YSN4_STRGA
Original site: A0A089YSN4_STRGA 
ID   A0A089YSN4_STRGA        Unreviewed;       406 AA.
AC   A0A089YSN4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:AIR96680.1};
GN   ORFNames=SGLAU_03260 {ECO:0000313|EMBL:AIR96680.1};
OS   Streptomyces glaucescens.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1907 {ECO:0000313|EMBL:AIR96680.1, ECO:0000313|Proteomes:UP000029482};
RN   [1] {ECO:0000313|Proteomes:UP000029482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40922 / GLA O {ECO:0000313|Proteomes:UP000029482};
RX   PubMed=25499805; DOI=10.1016/j.jbiotec.2014.11.036;
RA   Ortseifen V., Winkler A., Albersmeier A., Wendler S., Puhler A.,
RA   Kalinowski J., Ruckert C.;
RT   "Complete genome sequence of the actinobacterium Streptomyces glaucescens
RT   GLA.O (DSM 40922) consisting of a linear chromosome and one linear
RT   plasmid.";
RL   J. Biotechnol. 194:81-83(2015).
CC   -!- SIMILARITY: Belongs to the peptidase S11 family.
CC       {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP009438; AIR96680.1; -; Genomic_DNA.
DR   RefSeq; WP_052413588.1; NZ_CP009438.1.
DR   AlphaFoldDB; A0A089YSN4; -.
DR   STRING; 1907.SGLAU_03260; -.
DR   KEGG; sgu:SGLAU_03260; -.
DR   eggNOG; COG1686; Bacteria.
DR   HOGENOM; CLU_027070_3_1_11; -.
DR   OrthoDB; 3663940at2; -.
DR   Proteomes; UP000029482; Chromosome.
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:SF33; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACB1; 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:AIR96680.1};
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:AIR96680.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029482};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..406
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038748618"
FT   DOMAIN          67..298
FT                   /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00768"
FT   REGION          35..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          331..358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        336..350
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        100
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        103
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        158
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   BINDING         269
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ   SEQUENCE   406 AA;  41521 MW;  84F0119D1988AB7B CRC64;
     MTIGFSSRMS VATCGFCLVG VLGLAPAAVA ARAAADPGAP GGPAAAPRPS LLYRPGTHVR
     PRAGAPRLPD VSARSWLVAD ARTGEVLAAH DAHRKLPPAS TLKTLFALTV LPSLPGGIRH
     RVGPEELEGI GAGSSLVGVA EGRAYRVTDL WRGVFLSSGN DAVRVLAALN GGWRTTARRM
     QAKARSLGAL DTRVVSPDGY DAPGQVSSAY DLTVFGRAGL RSADFARYCA TVEADFPGRG
     GRVYPIRNTN RLLTGADGVE RYRGLIGVKN GYTSRAGHTL VAAARKGGRT LVVTVMNPRE
     GDGFAVYEEA RSLLDWGFGA AGRVDPVGSL DALRTPPRPG PDPAPAVPAG AAPGSGPGWA
     RPAAVVGAAG LGAGAVALVL RFLDALGLRG GRGGRAVRTP TDPSGS
//
DBGET integrated database retrieval system