ID A0A1Q5N454_9ACTN Unreviewed; 402 AA.
AC A0A1Q5N454;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:OKK21234.1};
GN ORFNames=AMK16_10915 {ECO:0000313|EMBL:OKK21234.1};
OS Streptomyces sp. CB00455.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703927 {ECO:0000313|EMBL:OKK21234.1, ECO:0000313|Proteomes:UP000185643};
RN [1] {ECO:0000313|EMBL:OKK21234.1, ECO:0000313|Proteomes:UP000185643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB00455 {ECO:0000313|EMBL:OKK21234.1,
RC ECO:0000313|Proteomes:UP000185643};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OKK21234.1}.
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; LIVQ01000002; OKK21234.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q5N454; -.
DR STRING; 1703927.AMK16_10915; -.
DR Proteomes; UP000185643; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF33; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACB1; 1.
DR Pfam; PF00768; Peptidase_S11; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000313|EMBL:OKK21234.1};
KW Hydrolase {ECO:0000313|EMBL:OKK21234.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:OKK21234.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000185643};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 368..387
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 65..299
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT REGION 9..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 402 AA; 41366 MW; 5B5A7BA30867E41B CRC64;
MVPAMFVAPA HAAPAPPAPP DGKGKPSRTR AAAAPPASMS TVGGALLGQP GTQVNLLPGA
PALPANLTGR SWIVADAESG EVLAAHNAHW RLPPASTMKM LFADTVLPRL PKDQVHKVTD
QDMDGVGPGS SLVGVKEDHE YSVHDLWLGV FLRSGNDAVH VLSAMNGGID KTVRDMQAHA
EELQALDTHV ISPDGYDAPE QVSSAYDLTL IARSGLAKQD FREYCGTAEA KFPGLQEPGK
ARDYFEIQNT NRLMTGAGGL SPYKGIAGVK NGNTTMAGST FTGVAQHGAR KLLVTVMNPD
GGGANEVYEE TAALFDWGFG AVGKVKPVGE LVPPKSADTT SQGSTAEAHE HGPAAAGAGS
GGGGAGTALG VAGGALALLA GGALVFNRRW PRGRRGRDED LV
//