ID   W5VYG2_9PSEU            Unreviewed;       444 AA.
AC   W5VYG2;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Peptidase M14 carboxypeptidase A domain-containing protein {ECO:0000259|SMART:SM00631};
GN   ORFNames=KALB_567 {ECO:0000313|EMBL:AHH93943.1};
OS   Kutzneria albida DSM 43870.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Kutzneria.
OX   NCBI_TaxID=1449976 {ECO:0000313|EMBL:AHH93943.1, ECO:0000313|Proteomes:UP000019225};
RN   [1] {ECO:0000313|EMBL:AHH93943.1, ECO:0000313|Proteomes:UP000019225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43870 {ECO:0000313|EMBL:AHH93943.1};
RX   PubMed=25301375; DOI=10.1186/1471-2164-15-885;
RA   Rebets Y., Tokovenko B., Lushchyk I., Ruckert C., Zaburannyi N.,
RA   Bechthold A., Kalinowski J., Luzhetskyy A.;
RT   "Complete genome sequence of producer of the glycopeptide antibiotic
RT   Aculeximycin Kutzneria albida DSM 43870T, a representative of minor genus
RT   of Pseudonocardiaceae.";
RL   BMC Genomics 15:885-885(2014).
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}.
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DR   EMBL; CP007155; AHH93943.1; -; Genomic_DNA.
DR   RefSeq; WP_025354216.1; NZ_CP007155.1.
DR   AlphaFoldDB; W5VYG2; -.
DR   STRING; 1449976.KALB_567; -.
DR   KEGG; kal:KALB_567; -.
DR   PATRIC; fig|1449976.3.peg.576; -.
DR   eggNOG; COG2866; Bacteria.
DR   HOGENOM; CLU_022371_0_0_11; -.
DR   OrthoDB; 5240362at2; -.
DR   Proteomes; UP000019225; Chromosome.
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   SMART; SM00631; Zn_pept; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000019225};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..444
FT                   /note="Peptidase M14 carboxypeptidase A domain-containing
FT                   protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004874737"
FT   DOMAIN          114..429
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|SMART:SM00631"
FT   REGION          237..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..256
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   444 AA;  46854 MW;  4844405BC7216500 CRC64;
     MAPRSLLRIA LGVTALLLPA AVLGGAAAAT PGDDTPLMWR VPVTGNQAAQ LVSAGFDVAE
     SGGDGSVFVV GNQTTATVLR QLGYQPTVHD TIYKDLPSAA EQRSLAGDTF YGGYHTVPAQ
     EAHLRQVASA HPDLATTYDV GDSWLKTKSK GGHDIQAICL TKKQSGDCEL TTNSKKPKFV
     LIAQIHAREI ATGELAWRWI DYLANGYGSD SQVKSILDST EVWVVPIANP DGVDIVASGG
     NSPKMQRKNA DNSRGGCTGT DVGIDLNRNS TFHWGGDSNS PCDETYQGQV KGSEPEVKGL
     ESFFRAIYPV QRGTGDNDPA PDTARGTMIT LHSYGNDIIV PWGWTEDPSP NDKALRALGQ
     KMAAGNGYVV DTNGGTVGYM TTGTTDDFTY GVLGVASYTI EVGPSSGGCG GFFPQFSCLD
     SKFWPEMKGA FTAAAVAAGA PYRQ
//