ID D5WWI5_KYRT2 Unreviewed; 359 AA.
AC D5WWI5;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Peptidase M42 family protein {ECO:0000313|EMBL:ADG07750.1};
GN OrderedLocusNames=Btus_3136 {ECO:0000313|EMBL:ADG07750.1};
OS Kyrpidia tusciae (strain DSM 2912 / NBRC 15312 / T2) (Bacillus tusciae).
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae; Kyrpidia.
OX NCBI_TaxID=562970 {ECO:0000313|EMBL:ADG07750.1, ECO:0000313|Proteomes:UP000002368};
RN [1] {ECO:0000313|Proteomes:UP000002368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2912 / NBRC 15312 / T2 {ECO:0000313|Proteomes:UP000002368};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Ovchinnikova G., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F.,
RA Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA Wu D., Pukall R., Schneider S., Wahrenburg C., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Bacillus tusciae DSM 2912.";
RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADG07750.1, ECO:0000313|Proteomes:UP000002368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2912 / NBRC 15312 / T2 {ECO:0000313|Proteomes:UP000002368};
RX PubMed=22180816; DOI=10.4056/sigs.2144922;
RA Klenk H.P., Lapidus A., Chertkov O., Copeland A., Del Rio T.G., Nolan M.,
RA Lucas S., Chen F., Tice H., Cheng J.F., Han C., Bruce D., Goodwin L.,
RA Pitluck S., Pati A., Ivanova N., Mavromatis K., Daum C., Chen A.,
RA Palaniappan K., Chang Y.J., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA Rohde M., Abt B., Pukall R., Goker M., Bristow J., Markowitz V.,
RA Hugenholtz P., Eisen J.A.;
RT "Complete genome sequence of the thermophilic, hydrogen-oxidizing Bacillus
RT tusciae type strain (T2) and reclassification in the new genus, Kyrpidia
RT gen. nov. as Kyrpidia tusciae comb. nov. and emendation of the family
RT Alicyclobacillaceae da Costa and Rainey, 2010.";
RL Stand. Genomic Sci. 5:121-134(2011).
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|PIRSR:PIRSR001123-2};
CC Note=Binds 2 divalent metal cations per subunit.
CC {ECO:0000256|PIRSR:PIRSR001123-2};
CC -!- SIMILARITY: Belongs to the peptidase M42 family.
CC {ECO:0000256|ARBA:ARBA00006272, ECO:0000256|PIRNR:PIRNR001123}.
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DR EMBL; CP002017; ADG07750.1; -; Genomic_DNA.
DR RefSeq; WP_013077029.1; NC_014098.1.
DR AlphaFoldDB; D5WWI5; -.
DR STRING; 562970.Btus_3136; -.
DR KEGG; bts:Btus_3136; -.
DR eggNOG; COG1363; Bacteria.
DR HOGENOM; CLU_047249_1_0_9; -.
DR OrthoDB; 9772053at2; -.
DR Proteomes; UP000002368; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.30.40; Peptidase M42, domain 2; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR008007; Peptidase_M42.
DR InterPro; IPR023367; Peptidase_M42_dom2.
DR PANTHER; PTHR32481; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR32481:SF0; AMINOPEPTIDASE YPDE-RELATED; 1.
DR Pfam; PF05343; Peptidase_M42; 1.
DR PIRSF; PIRSF001123; PepA_GA; 1.
DR SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001123-2}; Protease {ECO:0000256|ARBA:ARBA00022670}.
FT ACT_SITE 213
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 320
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 359 AA; 38779 MW; BEC023E3F2A87584 CRC64;
MNNWQGIDSF LELLALDGPS GHEDAVAIWL SHWFKAAGLT VEQDALGNLI ARRPAADPGD
DRPPTVLITA HMDEIGLMVS HIEAGGFLRF VPIGGVDPRT LPSAEVTVHG RKPLLGVIGS
KPPHLSTPEE RKEAAGTERM FIDLGLPELE VREWVRPGDP VTIRRRPLRL LDDRIAAKSV
DNRASVAAVF ECIAQLSSHP LQVDVVFAAT VQEEVGMRGA ATAAYQIRPD LAVAVDVCHA
RSPGVSTERT MGMGDGPAIQ FGPNIHPALF RSLTAATQAA GLPYQVLVAQ GATGTDARLM
QLCREGIPTA ALGIPIRYMH TSVETVQYQD IRRTGQLLAG WLKSLNRSVV EGFLCYFDV
//
