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Database: UniProt
Entry: A0A1I5C9K2_9MICO
LinkDB: A0A1I5C9K2_9MICO
Original site: A0A1I5C9K2_9MICO 
ID   A0A1I5C9K2_9MICO        Unreviewed;       853 AA.
AC   A0A1I5C9K2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:SFN83556.1};
GN   ORFNames=SAMN05216219_2289 {ECO:0000313|EMBL:SFN83556.1};
OS   Mycetocola miduiensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Mycetocola.
OX   NCBI_TaxID=995034 {ECO:0000313|EMBL:SFN83556.1, ECO:0000313|Proteomes:UP000198867};
RN   [1] {ECO:0000313|Proteomes:UP000198867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.11101 {ECO:0000313|Proteomes:UP000198867};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC       {ECO:0000256|ARBA:ARBA00026057}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; FOVM01000006; SFN83556.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5C9K2; -.
DR   STRING; 995034.SAMN05216219_2289; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000198867; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR028299; ClpA/B_CS2.
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; PS00871; CLPAB_2; 1.
DR   PROSITE; PS50151; UVR; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000313|EMBL:SFN83556.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SFN83556.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198867};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          37..178
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          451..486
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   COILED          466..493
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   853 AA;  92565 MW;  C0B2ED649458AEFD CRC64;
     MPPFFGPTGS ESESFDEFLA RYLQGQRAAQ SGRTIDITRL LSRRTQEVLA DAARFAVEHG
     HSEVDALHVL RVLLEKAPVA DAIQSLGADP EALAEAVEQR LPEKADRNVQ SASLTSSTQR
     ALMDAYQVAR AFGSTYIDPE HLFFAFVANQ EMPAGQLLAH FGITPQSLQA GYESARAAQA
     AGEAPGQSTA SATPMLDQFG TDLTARARDG KLDPVIGRAD EIAQTIEILS RRTKNNPVLI
     GEAGVGKTAV VEGLAQAIVD EDVPHLLRGK RVIALDLASM VGGTRYRGDF EERLTKLLDE
     ISTHQGELIV FVDELHTVVG AGGGGESGGM DAGNILKPRL ARGELHVVGA TTLKEYRRIE
     KDAALERRFQ PVNVNEPSVD DAEIILRGLR ERYEEFHDVS YTDEALRAAV DLSARYVTDR
     FLPDKAIDLL DQAGARLRLR QVAKIDTTEL REHVATLEAS KDAAVVAERY EEASRLRDEI
     EALTAQIAAV ESMDAAASAS VPAIVGEAEI AEIISRATGI PATRLTQGDR QRLGSLEAEL
     HERVIGQHDA VESIAKAVRR NRTGMGDPNR PVGSFLFLGP TGVGKTELAK ALASSLFGDD
     SAMLRFDMSE FGERHTVSRL VGAPPGYVGY DEAGQLTERV RRNPYSVILL DEIEKAHPDV
     FNLLLQVLDD GRLTDGQGRT VDFRNTVVIM TSNIGSEFLA SRSGALGFVA DSADGSGFGS
     EKALRDRVMG KLREAMRPEF LNRIDEVVLF RKLEQAQLHD IVRLLLTRTA SRLHAQGVEL
     NVSDAAVDWI ATSGYEPEYG ARPLRRVIQR EVEDRIAGLM VDTELSAGSS IAVSVVGDEL
     LVESHVLEPS LAA
//
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