ID A0A1P8XWN4_9ACTN Unreviewed; 532 AA.
AC A0A1P8XWN4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine-endopeptidase {ECO:0000313|EMBL:AQA12619.1};
GN ORFNames=BV401_21395 {ECO:0000313|EMBL:AQA12619.1};
OS Streptomyces autolyticus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=75293 {ECO:0000313|EMBL:AQA12619.1, ECO:0000313|Proteomes:UP000187851};
RN [1] {ECO:0000313|Proteomes:UP000187851}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC0516 {ECO:0000313|Proteomes:UP000187851};
RA Yin M., Jiang M., Lu T.;
RT "Streptomyces autolyticus CGMCC0516 complete genome sequence.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S13 family.
CC {ECO:0000256|ARBA:ARBA00006096}.
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; CP019458; AQA12619.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1P8XWN4; -.
DR STRING; 75293.BV401_21395; -.
DR KEGG; sauo:BV401_21395; -.
DR OrthoDB; 56883at2; -.
DR Proteomes; UP000187851; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 2.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR000667; Peptidase_S13.
DR NCBIfam; TIGR00666; PBP4; 1.
DR PANTHER; PTHR30023; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR30023:SF0; PENICILLIN-SENSITIVE CARBOXYPEPTIDASE A; 1.
DR Pfam; PF02113; Peptidase_S13; 2.
DR PRINTS; PR00922; DADACBPTASE3.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:AQA12619.1};
KW Hydrolase {ECO:0000313|EMBL:AQA12619.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:AQA12619.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 57..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 84..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 532 AA; 55476 MW; 7A7F024CDB48531A CRC64;
MPEARSWQVR EWLRHRLSRG RREFDRVRGR GLREWNRVRA RARREWRRTP REQQRTWQLV
AVSAATGLVV AVVSVLVAGP WDAGQRTAER ARAADGRAPG DGRDGGSGEP APSAAPVLAA
LGARSAPRSP DSGADAVPPP TGAGLADTLE PLLDDPALGD ERSVAVMDVT SGQQVFGAKA
GTATIPASTI KLATGAAALS ALGPDHRIRT SVVAGAGKND IVLVGGGDPT LTARAVKGDD
HPAALRQLAD DTARALKKRG GGTYRLGYDT SLYSGAKLHP IGPNENLSPV VPLMADEGRK
DDSDHGPAPR AEDPAADAAA TFASMLRDRG VEVKDEPRSR KAAKGARTVA SVRSQPLSSL
VERMLTTSDN DIAEALSRQT ALAAGRSASF EGGAKAVTQR LRKLGLPLGG ARIADGSGLD
RADHVSAGLL AQVLVRAADR DHPELRSLLT GLPVAGFSGT LRTRYAQDAV GRGVVRAKTG
TLTGVNSLAG SVVDADGRLL VFAFMTNGTT DANGAQRALD RMASALANCG CR
//
