ID A0A0M9ZLD5_9ACTN Unreviewed; 983 AA.
AC A0A0M9ZLD5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Peptidase M14 {ECO:0000313|EMBL:KOV62745.1};
GN ORFNames=ADL01_28765 {ECO:0000313|EMBL:KOV62745.1};
OS Streptomyces sp. NRRL WC-3618.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519490 {ECO:0000313|EMBL:KOV62745.1, ECO:0000313|Proteomes:UP000037738};
RN [1] {ECO:0000313|EMBL:KOV62745.1, ECO:0000313|Proteomes:UP000037738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL WC-3618 {ECO:0000313|EMBL:KOV62745.1,
RC ECO:0000313|Proteomes:UP000037738};
RA Noorani M.;
RL Submitted (JUL-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:KOV62745.1}.
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; LGDW01000443; KOV62745.1; -; Genomic_DNA.
DR RefSeq; WP_053744886.1; NZ_LGDW01000443.1.
DR AlphaFoldDB; A0A0M9ZLD5; -.
DR PATRIC; fig|1519490.3.peg.6267; -.
DR OrthoDB; 5240362at2; -.
DR Proteomes; UP000037738; 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 CDD; cd03859; M14_CPT; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR033810; Carboxypeptidase_T.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR PANTHER; PTHR11705:SF145; SLL0236 PROTEIN; 1.
DR Pfam; PF20773; InhA-like_MAM; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000037738};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..983
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005842975"
FT DOMAIN 172..194
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00132"
FT REGION 272..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 983 AA; 104086 MW; 744BFBC4AD447F74 CRC64;
MRRRARTILA VGALVLGGAG LAPIAVAAED AGTPGPDEVK VFRAEVTKAQ IPLLLAAGQD
GHELGEQAPD KGTATVEVYL TDKQADQLED KGVHLKEHTL TATARARVAA AGDGVFRPYS
GAGNLREEIL KTAQQNPGLT KVVSIGKTLR GQDILALKLT KGAKKTKDGA KPSVLYLSNQ
HAREWITPEM TRRLMHHYLD NYSRDKRIKK IVDSTELWFV LSANPDGYDF THRPDGDRQW
RKNMRDVNGD GNITIGDGVD LNRNFAYKWG YDDEGSSPSP TSETYRGAGP ASEPETKALD
AFEKRVGFTY GINYHSAAEL LLYGVGWQVA SPSPDDVLYK SLAGTPEKSA IPGYHPQLSS
ELYTTNGEAD GHAANVNGMG MFTPEMSTCQ TASNLYPDDA WKAADCASVF TFPDDEKLIQ
QEFAKNIPFA LSVAESAARP DQPKSSVGIA APDFTPAPFT TSYSRGADQE VSVVVRRSVR
DKELKYRVNG GRTEDMALKA WKGGETYGGD DNLYFDEYRA KVADGDPGDK VEVWFTGETK
AGKHTKSTRF TYTVAERPRA DTLVVAEEGA TATQAQTYVD ALKANGRKPL VWDVAALGAP
DALGVLRHFK TVVHYTGAVR PGNATQLQLR AYLNEGGKLV EAGESAGGSV DLGGGTLSND
FSQYYLGAYS RTTTPSVSAF NGSGKLTGFN GALGDAPGNP LNAAGSFGVT SDNLAAQTYP
QFASAGAGGY PGAANPYGPY AGASMAAVKH TDYAWNRLTR TIDLTGVSAA SAPTFRTQLL
WDTEEGYDHA VLEAHTAGAD DWTTLPEKGG ATSTAVPAEC EAGFFIKGHP ALTRYLTLGS
GACTPTGTSG SWNSFTGASA GWQQVNFDLS AYAGKKVEIS ISYITDPGSG GRGVLADNAT
VVIGGTAGPV EDFETSLGAW SVPGPPAGSP AVIKDWGLSG ELARTYGAVT TDDTVLLGFG
LEHVTAAADR KALLGKALAA LKD
//
