ID A0A0F0KY21_9MICO Unreviewed; 855 AA.
AC A0A0F0KY21;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:KJL25374.1};
GN Name=clpC {ECO:0000313|EMBL:KJL25374.1};
GN ORFNames=RL72_01442 {ECO:0000313|EMBL:KJL25374.1};
OS Microbacterium azadirachtae.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=582680 {ECO:0000313|EMBL:KJL25374.1, ECO:0000313|Proteomes:UP000033448};
RN [1] {ECO:0000313|EMBL:KJL25374.1, ECO:0000313|Proteomes:UP000033448}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23848 {ECO:0000313|EMBL:KJL25374.1,
RC ECO:0000313|Proteomes:UP000033448};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJL25374.1}.
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DR EMBL; JYIT01000070; KJL25374.1; -; Genomic_DNA.
DR RefSeq; WP_045250147.1; NZ_JYIT01000070.1.
DR AlphaFoldDB; A0A0F0KY21; -.
DR PATRIC; fig|582680.7.peg.1480; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000033448; Unassembled WGS sequence.
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 78, MITOCHONDRIAL; 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};
KW Hydrolase {ECO:0000313|EMBL:KJL25374.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:KJL25374.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033448};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 34..177
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 449..484
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 173..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 855 AA; 92328 MW; 1555A7297B4DC2CD CRC64;
MPNDFTDAGS GSFDEFLARY LAGEQARQTR SIDLSRFLTV RAQRMLQRAG RFALERGQTE
LDALHVLRTV VEDDAVDQAI RNIGVTPKAI VDAVEARLPA PADASDVEAA TITPGASRAL
FHAYQVARSS GATYIEPEHI FFALVLGQDA PAGQILARAG VTAEALTQSL REPVTAGAAP
EADATQPASE TPMLDRFGLD LTARARAGEL DPVIGRADEI EQTIEILSRR TKNNPVLIGE
AGVGKTAIVE GLARAIVDGA VPAPLKDRRV VALDLPAMLS GTRYRGDFEE RLTQTMDEIA
AHKGEIVVFI DEVHTVVGAG GSGEGGGMDA GNILKPRLAR GDLHLVGATT LAEYRRIEKD
PALERRFQPV KVAEPSIEDA VRILEGLKPA YEQHHAVTYT DDAVRAAVEL SARYLPDRVL
PDKAIDLIDQ AGARLRLRLG VVTDVAALFA ELADLEARKN AAVGAEHYEE ASRIRDEIAA
VQARIDDAGA PSPVSQTGDA IVDEAEIAAV IARATGIPVS RVSESERERL ADLEAELHAR
VIGQDDAVTA VARAVRRSRT GMGDARRPVG SFLFLGPTGV GKTELAKALA DRLLDDESAV
IRFDMSEFGE RHTVSRLVGA PPGYVGYDEA GQLTERVRRN PYSIVLFDEI EKAHPDVFNL
LLQVLDDGRL TDGQGRTVDF RNTVIVMTSN IGSEFLASRS GALGFVASQD ASANGFASQE
DLRARVMGKL REAMRPELLN RIDEIVLFQK LGREELGRIV RLLLQATERR LDGREVALDV
TDAAVAWLGE HGYEPEYGAR PLRRLIQREV DDRIADLFVS GELRDGGRVR VDAVDGALRV
TAPSEVAQAE PARAA
//
