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Database: UniProt
Entry: B2HM34_MYCMM
LinkDB: B2HM34_MYCMM
Original site: B2HM34_MYCMM 
ID   B2HM34_MYCMM            Unreviewed;       247 AA.
AC   B2HM34;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=ATP-dependent protease ATP-binding subunit ClpC2 {ECO:0000313|EMBL:ACC40498.1};
GN   Name=clpC2 {ECO:0000313|EMBL:ACC40498.1};
GN   OrderedLocusNames=MMAR_2048 {ECO:0000313|EMBL:ACC40498.1};
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium ulcerans group.
OX   NCBI_TaxID=216594 {ECO:0000313|EMBL:ACC40498.1, ECO:0000313|Proteomes:UP000001190};
RN   [1] {ECO:0000313|EMBL:ACC40498.1, ECO:0000313|Proteomes:UP000001190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M {ECO:0000313|Proteomes:UP000001190};
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA   Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA   Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA   Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum on the
RT   evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(2008).
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DR   EMBL; CP000854; ACC40498.1; -; Genomic_DNA.
DR   RefSeq; WP_012393825.1; NC_010612.1.
DR   AlphaFoldDB; B2HM34; -.
DR   STRING; 216594.MMAR_2048; -.
DR   KEGG; mmi:MMAR_2048; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_083296_0_0_11; -.
DR   OrthoDB; 3290891at2; -.
DR   Proteomes; UP000001190; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   InterPro; IPR036628; Clp_N_dom_sf.
DR   InterPro; IPR004176; Clp_R_dom.
DR   Pfam; PF02861; Clp_N; 2.
DR   SUPFAM; SSF81923; Double Clp-N motif; 1.
DR   PROSITE; PS51903; CLP_R; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000313|EMBL:ACC40498.1};
KW   Hydrolase {ECO:0000313|EMBL:ACC40498.1};
KW   Nucleotide-binding {ECO:0000313|EMBL:ACC40498.1};
KW   Protease {ECO:0000313|EMBL:ACC40498.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001190};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          96..238
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          216..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   247 AA;  26336 MW;  E8535D72BB2BDF30 CRC64;
     MAESTKITYP VRLDELIDAI KQVHTNALDQ LTDAVLAAEH LGEIADHLIG HFVDQARRSG
     ASWTDIGKSM GVTKQAAQKR FVPRAEATTL DPEQGFGRFT PRARSAVVAA QNAAHQGAND
     EITPDHLLLG VLADPAALAT ALLRMQAIDT EALRASVRLP AATGETPALI PFSGPARKVL
     ELTFREALRL GHNYIGTEHM LLALLELEDG AGPLHRSGVE KSRAEADLSS ALESLTGHGP
     DSRPGKS
//
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