ID R7RTK4_9CLOT Unreviewed; 371 AA.
AC R7RTK4;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Aminopeptidase {ECO:0000313|EMBL:CDF58560.1};
GN ORFNames=TCEL_00606 {ECO:0000313|EMBL:CDF58560.1};
OS Thermobrachium celere DSM 8682.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Thermobrachium.
OX NCBI_TaxID=941824 {ECO:0000313|EMBL:CDF58560.1, ECO:0000313|Proteomes:UP000014923};
RN [1] {ECO:0000313|EMBL:CDF58560.1, ECO:0000313|Proteomes:UP000014923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8682 {ECO:0000313|EMBL:CDF58560.1,
RC ECO:0000313|Proteomes:UP000014923};
RA Ciranna A., Larjo A., Kivisto A., Santala V., Roos C., Karp M.;
RT "Draft genome sequence of the hydrogen-ethanol-producing anaerobic
RT alkalithermophilic Caloramator celere.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M29 family.
CC {ECO:0000256|ARBA:ARBA00008236}.
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:CDF58560.1}.
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DR EMBL; CAVN010000097; CDF58560.1; -; Genomic_DNA.
DR RefSeq; WP_018662777.1; NZ_HF952018.1.
DR AlphaFoldDB; R7RTK4; -.
DR eggNOG; COG2309; Bacteria.
DR HOGENOM; CLU_057697_0_0_9; -.
DR OrthoDB; 9803993at2; -.
DR Proteomes; UP000014923; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1830.10; Thermophilic metalloprotease (M29); 1.
DR InterPro; IPR035097; M29_N-terminal.
DR InterPro; IPR000787; Peptidase_M29.
DR PANTHER; PTHR34448; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR34448:SF1; BLL6088 PROTEIN; 1.
DR Pfam; PF02073; Peptidase_M29; 1.
DR SUPFAM; SSF144052; Thermophilic metalloprotease-like; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:CDF58560.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000014923}.
SQ SEQUENCE 371 AA; 41814 MW; FEBF8B07D5935EDA CRC64;
MVDPRITTLA HNLINYSCRL KEGEKVLIES IGLELPLVKE LVKEAYKVGA IPFVTIKNKS
VDRAILMGAT EEQMKMMAKY EAARMSDMDA YIGIRSGDNA SELSDVPADK MDLYFKYFWK
EVHGNIRVPK TKWVVLRYPS PSMAQLANTS TEAFEDFYFN VCNLDYSKMS KAMDPLVELM
SKTDKVRIVG PGTDLTFSIK GIPVVKCDGK MNIPDGEVYT APVKDSVNGY ITYNTPAEYQ
GFTYENIRLE FKDGKIVKAT ANDTERINKV FDTDEGARYI GEFAIGVNPY ITKPMKDTLF
DEKITGSIHF TPGSSYDDAF NGNKSAIHWD LVYIQTPEYG GGEIYFDDVL IRKDGRFVLP
ELEGLNPENL K
//
