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Database: UniProt
Entry: A0A285QVF1_9ACTN
LinkDB: A0A285QVF1_9ACTN
Original site: A0A285QVF1_9ACTN 
ID   A0A285QVF1_9ACTN        Unreviewed;       460 AA.
AC   A0A285QVF1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase (Penicillin-binding protein 5/6) {ECO:0000313|EMBL:SOB85806.1};
GN   ORFNames=SAMN06272789_6107 {ECO:0000313|EMBL:SOB85806.1};
OS   Streptomyces sp. 1331.2.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1938835 {ECO:0000313|EMBL:SOB85806.1, ECO:0000313|Proteomes:UP000219030};
RN   [1] {ECO:0000313|Proteomes:UP000219030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1331.2 {ECO:0000313|Proteomes:UP000219030};
RA   Varghese N., Submissions S.;
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; OBMJ01000001; SOB85806.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285QVF1; -.
DR   Proteomes; UP000219030; Unassembled WGS sequence.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
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   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000313|EMBL:SOB85806.1};
KW   Hydrolase {ECO:0000313|EMBL:SOB85806.1};
KW   Protease {ECO:0000313|EMBL:SOB85806.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           37..460
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012718664"
FT   DOMAIN          70..297
FT                   /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00768"
FT   REGION          350..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          417..460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..460
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   460 AA;  47351 MW;  99779F34D6D7E6A0 CRC64;
     MPPKRVQQKS PYVTRAAAGA AATALVLAVG TPIALAALEQ DAAGPVGGER LARPDVQVAP
     LPGAPALPSA LSGRSWLVAD ATTGEVLAAR NAHLQLPPAS TLKMLFADTV MPKFDRSLEH
     QVTPAELANL GAGSSLVGVK ENLPYRVEDL WRGVFLSSGN DAVHVLAHMN GGIARTVAEM
     QARAGTLQAK DTKVVSPDGY DMDGQVSSAY DLTLFARAGL RNADFRSYCA TRTARFPGGL
     DQLTGQRTSF DIANTDRLLG KYPGLIGVKN GYTTNAGATF TGAAERDGRT LLVTVMHPEA
     QGKVYDEAAS LLDWGFAAAG KVQPVGQLVE DTAPPASAAA SSSASAKASS APEAAAASQL
     PPWGRPPVAS GDTPGLAPAL WTGAVLATAL AAWATAHAGA RRRAAAAPAV TVSAPQRGGV
     RAAGGSSGVG GRSHRRLARR ARALVHSARS TRSVRTRQHR
//
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