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Database: UniProt
Entry: Q8FMH5_COREF
LinkDB: Q8FMH5_COREF
Original site: Q8FMH5_COREF 
ID   Q8FMH5_COREF            Unreviewed;       927 AA.
AC   Q8FMH5; C8NK17;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   24-JAN-2024, entry version 130.
DE   SubName: Full=Putative endopeptidase Clp ATP-binding chain C {ECO:0000313|EMBL:BAC19339.1};
OS   Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS   / NBRC 100395).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=196164 {ECO:0000313|EMBL:BAC19339.1, ECO:0000313|Proteomes:UP000001409};
RN   [1] {ECO:0000313|EMBL:BAC19339.1, ECO:0000313|Proteomes:UP000001409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395
RC   {ECO:0000313|Proteomes:UP000001409};
RX   PubMed=12840036; DOI=10.1101/gr.1285603;
RA   Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA   Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT   "Comparative complete genome sequence analysis of the amino acid
RT   replacements responsible for the thermostability of Corynebacterium
RT   efficiens.";
RL   Genome Res. 13:1572-1579(2003).
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DR   EMBL; BA000035; BAC19339.1; -; Genomic_DNA.
DR   RefSeq; WP_006769109.1; NZ_GG700685.1.
DR   AlphaFoldDB; Q8FMH5; -.
DR   STRING; 196164.gene:10742976; -.
DR   KEGG; cef:CE2529; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_1_11; -.
DR   OMA; ERMKAVM; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000001409; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 2.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 4.10.860.10; UVR domain; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR036628; Clp_N_dom_sf.
DR   InterPro; IPR004176; Clp_R_dom.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR018368; ClpA/B_CS1.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001943; UVR_dom.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 104; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF02861; Clp_N; 2.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF81923; Double Clp-N motif; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51903; CLP_R; 1.
DR   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS50151; UVR; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:BAC19339.1};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001409};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          2..144
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          443..478
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          145..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          868..927
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          439..485
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        885..901
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   927 AA;  101660 MW;  8997ECE721F88706 CRC64;
     MFERFTDRAR RVIVLAQEEA RMLNHNYIGT EHILLGLIHE GEGVAAKALE SMGISLDAVR
     QEVEEIIGHG SKPTTGHIPF TPRAKKVLEL SLREGLQMGH KYIGTEFLLL GLIREGEGVA
     AQVLVKLGAD LPRVRQQVIQ LLSGYEGGQG GSPDSPQGGQ GGDAVGAGSA PGGRATGSGA
     GERSNSLVLD QFGRNLTQAA KDGKLDPVVG RDKEIERIMQ VLSRRTKNNP VLIGEPGVGK
     TAVVEGLALD IVNGKVPETL KDKQVYSLDL GSLVAGSRYR GDFEERLKKV LKEINQRGDI
     ILFIDEIHTL VGAGAAEGAI DAASLLKPKL ARGELQTIGA TTLDEYRKHI EKDAALERRF
     QPVQVPEPSV ELSIEILKGL RDRYEAHHRV SITDGALVAA AQLSDRYIND RFLPDKAVDL
     IDEAGARMRI KRMTAPESLR EVDERIADVR REKEAAIDAQ DFEKAAGLRD KERKLGEERA
     EKEKQWRSGD LEEIAEVGEE QIAEVLATWT GIPVFKLTEA ESSRLLNMEE ELHKRIIGQD
     EAVKAVSRAI RRTRAGLKDP KRPSGSFIFA GPSGVGKTEL SKALAEFLFG DDDSLIQIDM
     GEFHDRFTAS RLFGAPPGYV GYEEGGQLTE KVRRKPFSVV LFDEIEKAHK EIYNTLLQVL
     EDGRLTDGQG RIVDFKNTVL IFTSNLGTQD ISKAVGLGFS GSNETDSDAQ YDRMKNKVHD
     ELKKHFRPEF LNRIDEIVVF HQLTREQIIQ MVELLIGRVS RALADKDMGI ELTDKAKALL
     ASRGFDPVLG ARPLRRTIQR EIEDAMSEKI LFGEIGAGEI VTVDVDGWDG ESKNTDGATF
     TFTPRPKPLP DGKFSEISVE AAEAIQDVDS AADGDVPETG SLDGIDPETL RELDEDASSN
     PTESERVTGD YYGTDDQPGG AAPQREQ
//
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