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Database: UniProt
Entry: A0A127FB71_STEDE
LinkDB: A0A127FB71_STEDE
Original site: A0A127FB71_STEDE 
ID   A0A127FB71_STEDE        Unreviewed;       577 AA.
AC   A0A127FB71;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Cytosol aminopeptidase domain-containing protein {ECO:0000259|Pfam:PF00883};
GN   ORFNames=ACG33_11200 {ECO:0000313|EMBL:AMN47656.1};
OS   Steroidobacter denitrificans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Steroidobacterales;
OC   Steroidobacteraceae; Steroidobacter.
OX   NCBI_TaxID=465721 {ECO:0000313|EMBL:AMN47656.1, ECO:0000313|Proteomes:UP000070250};
RN   [1] {ECO:0000313|EMBL:AMN47656.1, ECO:0000313|Proteomes:UP000070250}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18526 {ECO:0000313|EMBL:AMN47656.1,
RC   ECO:0000313|Proteomes:UP000070250};
RA   Yang F.-C., Chen Y.-L., Yu C.-P., Tang S.-L., Wang P.-H., Ismail W.,
RA   Wang C.-H., Yang C.-Y., Chiang Y.-R.;
RT   "A Comprehensive Approach to Explore the Metabolic and Phylogenetic
RT   Diversity of Bacterial Steroid Degradation in the Environment: Testosterone
RT   as an Example.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M17 family.
CC       {ECO:0000256|ARBA:ARBA00009528}.
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DR   EMBL; CP011971; AMN47656.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A127FB71; -.
DR   STRING; 465721.ACG33_11200; -.
DR   KEGG; sdf:ACG33_11200; -.
DR   Proteomes; UP000070250; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR011356; Leucine_aapep/pepB.
DR   InterPro; IPR000819; Peptidase_M17_C.
DR   PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR   PANTHER; PTHR11963:SF23; ZGC:152830; 1.
DR   Pfam; PF00883; Peptidase_M17; 1.
DR   PRINTS; PR00481; LAMNOPPTDASE.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070250}.
FT   DOMAIN          216..540
FT                   /note="Cytosol aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00883"
FT   REGION          551..577
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        562..577
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   577 AA;  62431 MW;  F83701695EC71470 CRC64;
     MPVKESHLVE LLPAQRNIRI LQERAEFTDN MLRTHDAAIM VCEHEHAEIL LEKLPLGSTW
     RQLYRQAKAA GPVGVLVTSL TIANTPSTRG SARAAGSARA NGRAPGQARV LPLVLAFAKA
     DLSAFERLNL AARAWKALAA PSGARIVLSA HGLAPASAAG MLEALLAAAL AGSAPMPTCK
     SQPRDKNTPS RFILAGATAE KVDTARCNAI DRGNHLARWL TMLPPNVLDS ANYPRILRRL
     ARQHGWQCSF LDETALRRLG AGAFLAVSRA NRHRRAGIVR LHYRGTGRRA AAAETLRSLA
     LVGKGICFDT GGINLKTHKG MYRMHEDMQG SAVAVGTLLA LSELKVPYDI DCWLAITENE
     IGAHAFRPQE VVQAANGTSI QIVHSDAEGR MVLADTLALA AGARRISRTG MPAARRPDLL
     IDFATLTGAC IGALTERYSG IFTNRADWNG VLERHGRDCG ERVWPFPMDE DFDSELESPI
     ADILQCAMDG KGDHILAARF LNRFVPAEIP WIHLDLAAAN RTGGLGHIPT DCTGFGVRYV
     TTLLLERSLW PPHGTARRPR TRRAPATTSN TRIGAST
//
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