ID A0A263CX01_9PSEU Unreviewed; 598 AA.
AC A0A263CX01;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:OZM70509.1};
GN ORFNames=CFN78_25480 {ECO:0000313|EMBL:OZM70509.1};
OS Amycolatopsis antarctica.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=1854586 {ECO:0000313|EMBL:OZM70509.1, ECO:0000313|Proteomes:UP000242444};
RN [1] {ECO:0000313|EMBL:OZM70509.1, ECO:0000313|Proteomes:UP000242444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU-G6 {ECO:0000313|EMBL:OZM70509.1,
RC ECO:0000313|Proteomes:UP000242444};
RA Wang J., Leiva S., Huang J., Huang Y.;
RT "Amycolatopsis antarcticus sp. nov., isolated from the surface of an
RT Antarcticus brown macroalga.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase C40 family.
CC {ECO:0000256|ARBA:ARBA00007074}.
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:OZM70509.1}.
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DR EMBL; NKYE01000020; OZM70509.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A263CX01; -.
DR InParanoid; A0A263CX01; -.
DR OrthoDB; 1099523at2; -.
DR Proteomes; UP000242444; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd14814; Peptidase_M15; 1.
DR Gene3D; 3.30.1380.10; -; 1.
DR Gene3D; 3.90.1720.10; endopeptidase domain like (from Nostoc punctiforme); 1.
DR InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
DR InterPro; IPR000064; NLP_P60_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR003709; Pept_M15B.
DR PANTHER; PTHR34385; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR34385:SF1; PEPTIDOGLYCAN L-ALANYL-D-GLUTAMATE ENDOPEPTIDASE CWLK; 1.
DR Pfam; PF00877; NLPC_P60; 1.
DR Pfam; PF02557; VanY; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF55166; Hedgehog/DD-peptidase; 1.
DR PROSITE; PS51935; NLPC_P60; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:OZM70509.1};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:OZM70509.1};
KW Protease {ECO:0000313|EMBL:OZM70509.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000242444};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..598
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012763204"
FT DOMAIN 303..428
FT /note="NlpC/P60"
FT /evidence="ECO:0000259|PROSITE:PS51935"
FT REGION 27..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 64..105
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 188..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 598 AA; 61125 MW; CBB66BEEE913099D CRC64;
MRARALRLSA VLPVVSALAL TLAAAPAGAQ PPAQPPEPRL EAGVAPGAAT PDPRPGEAFA
GPELARLQRT AAEVQRELDD LAGLARSAQD SATEAAAELA RAAAERRAAD QAVLAQQQEV
DDYSRRVFTA MGRPDQLRLA MTVDNPRDLL DGTSLVRSLT EAQDRRLLGA MDRQRAARDA
ESAAAGVERT AAERKADVQR REGDATNRAD AVSAELTAPI DEANAAVVAQ QRAQADRNAA
TAANWKAYTD RLAAAGISPP PASRLRDPAA LPPGLSPSTG SAGAAQAGVA EATDAGERLL
VLPEETVAAV TAGIAALGLP YVPGESGAGP RAYSCDGLVH AVYGGLGVPA AAAEQFATGV
PVPPADVRPG DLVFLGPARY GVQSVGIVLD ERTMLAADAR LAGVVVTDLP TAADVLGASR
PALGARQAEP VPARADGELT WRCGGVELPA GTRGAGGGAA VGPWGGFPNG LIPATALCPI
GAGSHSLRCD AAQSFQALSQ AYAGVFGAPV CVTDSYRTFD GQVDLYRRKP SLAAVPGTSN
HGWGLAVDLC GGAESFGTAQ HGWLLANARA FGWVHPGWAR QGGGREEPWH WEFAGATG
//