ID A0A0Q8PY33_9ACTN Unreviewed; 272 AA.
AC A0A0Q8PY33;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Peptidase M14 carboxypeptidase A domain-containing protein {ECO:0000259|SMART:SM00631};
GN ORFNames=ASE01_14200 {ECO:0000313|EMBL:KRB76170.1};
OS Nocardioides sp. Root190.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736488 {ECO:0000313|EMBL:KRB76170.1, ECO:0000313|Proteomes:UP000050886};
RN [1] {ECO:0000313|EMBL:KRB76170.1, ECO:0000313|Proteomes:UP000050886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root190 {ECO:0000313|EMBL:KRB76170.1,
RC ECO:0000313|Proteomes:UP000050886};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB76170.1, ECO:0000313|Proteomes:UP000050886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root190 {ECO:0000313|EMBL:KRB76170.1,
RC ECO:0000313|Proteomes:UP000050886};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
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:KRB76170.1}.
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DR EMBL; LMIA01000010; KRB76170.1; -; Genomic_DNA.
DR RefSeq; WP_056753704.1; NZ_LMIA01000010.1.
DR AlphaFoldDB; A0A0Q8PY33; -.
DR STRING; 1736488.ASE01_14200; -.
DR OrthoDB; 5240362at2; -.
DR Proteomes; UP000050886; Unassembled WGS sequence.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11705:SF91; CARBOXYPEPTIDASE A1 (PANCREATIC)-RELATED; 1.
DR PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000050886};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..272
FT /note="Peptidase M14 carboxypeptidase A domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006352702"
FT DOMAIN 38..270
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|SMART:SM00631"
SQ SEQUENCE 272 AA; 29507 MW; 9BA196DC7D7F6AA1 CRC64;
MPGRLGLALT TLAATLAVAA GATVPVPATA VPVARTASVE RAVAAQAAAP YLERIVSIGK
SVRGRPIHAH YRGAKDPEHV LVVIGQMHGE EDAGRSTAGW IRRNARPLPG TGVWTILTMN
PDGDARNRRV NAHGVDLNRN WPTSGWTRAG RGTRYWGGPR RASEPETRAM MDFLTTVRPD
YIVSIHQPLN GIGRNNIDVA WEKRLSANLR LPRRYFGVGN PSGTVSPTMT GWYNDRRGHF
GVATTVEYAA RTSSTYRNSF AGRGILRAAR IS
//