ID A0A1R4IP68_9MICO Unreviewed; 727 AA.
AC A0A1R4IP68;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=ClpB protein {ECO:0000313|EMBL:SJN21548.1};
GN ORFNames=FM119_02845 {ECO:0000313|EMBL:SJN21548.1};
OS Mycetocola reblochoni REB411.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Mycetocola.
OX NCBI_TaxID=1255698 {ECO:0000313|EMBL:SJN21548.1, ECO:0000313|Proteomes:UP000196778};
RN [1] {ECO:0000313|Proteomes:UP000196778}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EB411 {ECO:0000313|Proteomes:UP000196778};
RA Dridi B.;
RL Submitted (FEB-2017) 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; FUKR01000017; SJN21548.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R4IP68; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000196778; 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 CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
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 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; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000196778};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 55..199
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 454..653
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 621..712
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT COILED 269..349
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 727 AA; 80125 MW; DDB494BF436B33A5 CRC64;
MANMQGAPSS QEEPMSALEQ YGVDLTEIAR SGKLDPVIGR DAEIRRVSQV LTRRTKNNPV
LIGEPGVGKT AVVEGLAQRI VAGDVAESLK DKRLVSLDLA ALVAGAKYRG EFEERLKAVL
QEINDAEGEV ITFIDELHTL MGAGGGEGSV AAANMLKPML ARGELRLIGA TTLDEYREYI
EKDAAMERRF QQVYVGEPSV EDTIAILRGL KERYEAHHKV AISDSALVAA AALSNRYIPS
RQLPDKAIDL IDEAASRLRM EIDSAPVEID ELRRGVDRLK LEELALKKEK DDASKERLAT
LRSTLAEREE RLAGLQQRWE RERSQLNRVG ELKGRLDQLR GEAERAQREG NLERASRLLY
GEIPVIQREL IEAEKAENSE PTMVNDQVTS DDIAEVIAAW TGIPVGRLLQ GETEKLLALE
SELHRRLIGQ DQAVEAVADA VRRTRAGISD PDRPTGSFLF LGPTGVGKTE LAKALADFLF
DDEKALVRID MSEYGEKHSV SRLVGAPPGY VGYEAGGQLT EAVRRRPYSV VLLDEVEKAH
PEVFDVLLQV LDDGRLTDGQ GRTVDFRNTI LVLTSNLGSQ YLVDASLTPE QKEEAVQQVV
RQAFKPEFVN RLDDIVVFSA LSQDDLGQIV ELYIDRLQRR LSDRRLELAV TPDARAWLAE
RGYDPVYGAR PLRRLMQKEI DDRLATALLA GRITDGDTVR VDLDGAGESL TVGRVATADP
AADGLGG
//