ID B5YJ33_THEYD Unreviewed; 354 AA.
AC B5YJ33;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Aminopeptidase P {ECO:0000313|EMBL:ACI21713.1};
GN OrderedLocusNames=THEYE_A0401 {ECO:0000313|EMBL:ACI21713.1};
OS Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87).
OC Bacteria; Nitrospirota; Thermodesulfovibrionia; Thermodesulfovibrionales;
OC Thermodesulfovibrionaceae; Thermodesulfovibrio.
OX NCBI_TaxID=289376 {ECO:0000313|EMBL:ACI21713.1, ECO:0000313|Proteomes:UP000000718};
RN [1] {ECO:0000313|Proteomes:UP000000718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51303 / DSM 11347 / YP87
RC {ECO:0000313|Proteomes:UP000000718};
RA Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT "The complete genome sequence of Thermodesulfovibrio yellowstonii strain
RT ATCC 51303 / DSM 11347 / YP87.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACI21713.1, ECO:0000313|Proteomes:UP000000718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51303 / DSM 11347 / YP87
RC {ECO:0000313|Proteomes:UP000000718};
RX PubMed=25635016;
RA Bhatnagar S., Badger J.H., Madupu R., Khouri H.M., O'Connor E.M.,
RA Robb F.T., Ward N.L., Eisen J.A.;
RT "Genome Sequence of the Sulfate-Reducing Thermophilic Bacterium
RT Thermodesulfovibrio yellowstonii Strain DSM 11347T (Phylum Nitrospirae).";
RL Genome Announc. 3:0-0(2015).
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DR EMBL; CP001147; ACI21713.1; -; Genomic_DNA.
DR RefSeq; WP_012546421.1; NC_011296.1.
DR RefSeq; YP_002248248.1; NC_011296.1.
DR AlphaFoldDB; B5YJ33; -.
DR STRING; 289376.THEYE_A0401; -.
DR EnsemblBacteria; ACI21713; ACI21713; THEYE_A0401.
DR KEGG; tye:THEYE_A0401; -.
DR PATRIC; fig|289376.4.peg.396; -.
DR eggNOG; COG0006; Bacteria.
DR HOGENOM; CLU_017266_4_2_0; -.
DR InParanoid; B5YJ33; -.
DR OrthoDB; 9806388at2; -.
DR Proteomes; UP000000718; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:UniProt.
DR GO; GO:0046914; F:transition metal ion binding; IEA:UniProt.
DR CDD; cd01092; APP-like; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 1.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000587; Creatinase_N.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR001714; Pept_M24_MAP.
DR PANTHER; PTHR46112; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR46112:SF3; AMINOPEPTIDASE YPDF; 1.
DR Pfam; PF01321; Creatinase_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR PRINTS; PR00599; MAPEPTIDASE.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
PE 4: Predicted;
KW Aminopeptidase {ECO:0000313|EMBL:ACI21713.1};
KW Hydrolase {ECO:0000313|EMBL:ACI21713.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:ACI21713.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000718};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 33..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 21..129
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 137..338
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
SQ SEQUENCE 354 AA; 40280 MW; E5E695F579879863 CRC64;
MANKYENRVK KVFDKISSYS EAFLVTNLKN IRYLTGFKGT FAIALLTWTG CYIFVDFRYS
EQAKKEATGE IICFKDSWID TLKKLIEEMH IKKLSFEVTC TYETFLKLRD NTKLELVPEH
YVIENIRAVK EDEEINNIKE AIKIAENAFL QNKHIIKEGI TEKTIAKMVE NTIKEHSDSL
PFPVIVASGE NSSMPHWRHS NRILKRGDFV IIDWGAEYNG YFCDMTRTFI IGEASEKQKE
IYEIVNNANL QAIETCRVDI EAKGIDAVAR NLIKQSGYGE NFGHATGHGV GLDVHELPKI
SAQSEETIKP GMIFTIEPGI YIEGFGGVRI EDMVAVKENS VEVLTTLSKD LEIL
//
