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Database: UniProt
Entry: F2NPT6_MARHT
LinkDB: F2NPT6_MARHT
Original site: F2NPT6_MARHT 
ID   F2NPT6_MARHT            Unreviewed;       357 AA.
AC   F2NPT6;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Peptidase M29 aminopeptidase II {ECO:0000313|EMBL:AEB12862.1};
GN   OrderedLocusNames=Marky_2139 {ECO:0000313|EMBL:AEB12862.1};
OS   Marinithermus hydrothermalis (strain DSM 14884 / JCM 11576 / T1).
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Marinithermus.
OX   NCBI_TaxID=869210 {ECO:0000313|EMBL:AEB12862.1, ECO:0000313|Proteomes:UP000007030};
RN   [1] {ECO:0000313|EMBL:AEB12862.1, ECO:0000313|Proteomes:UP000007030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14884 / JCM 11576 / T1 {ECO:0000313|Proteomes:UP000007030};
RX   PubMed=22675595; DOI=10.4056/sigs.2435521;
RA   Copeland A., Gu W., Yasawong M., Lapidus A., Lucas S., Deshpande S.,
RA   Pagani I., Tapia R., Cheng J.F., Goodwin L.A., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Pan C., Brambilla E.M., Rohde M., Tindall B.J., Sikorski J.,
RA   Goker M., Detter J.C., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Woyke T.;
RT   "Complete genome sequence of the aerobic, heterotroph Marinithermus
RT   hydrothermalis type strain (T1(T)) from a deep-sea hydrothermal vent
RT   chimney.";
RL   Stand. Genomic Sci. 6:21-30(2012).
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}.
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DR   EMBL; CP002630; AEB12862.1; -; Genomic_DNA.
DR   RefSeq; WP_013704907.1; NC_015387.1.
DR   AlphaFoldDB; F2NPT6; -.
DR   STRING; 869210.Marky_2139; -.
DR   KEGG; mhd:Marky_2139; -.
DR   eggNOG; COG2309; Bacteria.
DR   HOGENOM; CLU_057697_0_0_0; -.
DR   OrthoDB; 9803993at2; -.
DR   Proteomes; UP000007030; Chromosome.
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:AEB12862.1}; 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:UP000007030}.
SQ   SEQUENCE   357 AA;  39212 MW;  AEB7EDB7EDD71269 CRC64;
     MERRFAELLV DYCLEAQPGQ NVLLEAGTAA LPLVEALYSA LLQRGAYPFV KLSYPGQDAD
     FFQGAGAWLE RVPPVEVAVM EAVDASLRVI SAENPLDLAD VDPESLARHR KAWRPLSEAR
     LRKRWSLTLY PTAGFAQQAG MSTRAFRRFV ERALFLDHPD PIAAWRELSA FQDRLIARLA
     EAREIRVVAP GTDIRLGVAG RTWINSDGKR NMPSGEVFTA PHEDAVEGEI RFNLPAVVSG
     QRVEGIYLRF EGGEVVEARA RQGEAYLLRM LEADAGARRL GEFGIGTNFG IDRPTGIVLF
     DEKIGGTVHF ALGNAYPESG GRNASAVHWD IVLDLRSGGK ILVDGAVLQE DGRFVEG
//
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