ID A0A0K9XK96_9ACTN Unreviewed; 498 AA.
AC A0A0K9XK96;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:KNB53713.1};
GN ORFNames=AC230_03630 {ECO:0000313|EMBL:KNB53713.1};
OS Streptomyces caatingaensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1678637 {ECO:0000313|EMBL:KNB53713.1, ECO:0000313|Proteomes:UP000037288};
RN [1] {ECO:0000313|Proteomes:UP000037288}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMAA 1322 {ECO:0000313|Proteomes:UP000037288};
RA Santos S.N., Gacesa R., Taketani R.G., Long P.F., Melo I.S.;
RT "Draft genome sequence of Streptomyces sp. CMAA 1322, a bacterium isolated
RT from Caatinga biome, from dry forest semiarid of Brazil.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28A subfamily.
CC {ECO:0000256|ARBA:ARBA00005957}.
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:KNB53713.1}.
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; LFXA01000002; KNB53713.1; -; Genomic_DNA.
DR RefSeq; WP_049714438.1; NZ_LFXA01000002.1.
DR AlphaFoldDB; A0A0K9XK96; -.
DR STRING; 1678637.AC230_03630; -.
DR PATRIC; fig|1678637.3.peg.797; -.
DR Proteomes; UP000037288; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd03876; M28_SGAP_like; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 2.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR041756; M28_SGAP-like.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR PANTHER; PTHR12147:SF55; PEPTIDE HYDROLASE; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Hydrolase {ECO:0000313|EMBL:KNB53713.1};
KW Protease {ECO:0000256|ARBA:ARBA00022438};
KW Reference proteome {ECO:0000313|Proteomes:UP000037288};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..498
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005532695"
FT DOMAIN 157..239
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 265..483
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 498 AA; 52559 MW; 56293CAC2325FBC0 CRC64;
MRLPHRPGGR RALTALVATA VAAPVLLAAA PADARGTDDP ARQHRKAERL ARQLERESSA
RSAYRHLAAF QRIADANGGN RAAGTPGHDA SARYVYRLLE QAGYRVSSQD FTIWDARTTT
EKLSVLSPGP RELKVTAGKL SPSTPASGIQ AAIAVAKVSD KPGCTPDDYA SDTFTGKIAL
IKRGVCSYAE KQAAAAKAGA IGAVIYNHSG TAPARLRFDD PAEGRIPTAG ISLADGEALA
AAAAKGPVKL SLTIQQQHIP KTTRNVVAET RGGDANHVVA LGSHLDSVPE GPGINDNGSG
SAGLLEVALK LARTTRHPTN KVRFAWWSGE ELGLLGSDHY VKQLTPEQRR KIALYLNFDM
IASPNAAELV YDGDDSDHKG SGPGPKGSAE IEKLITDYLD RKHKPHEGTD FDGRSDYGPF
IDAGIPAGGT FTGAEGIKTE EQAAKFGGTA GVAYDPNYHA KGDTLKNIDL KYFDTNIDVI
AHAVGVYAHD LGSLGTRN
//
