ID K1Z6A6_9BACT Unreviewed; 866 AA.
AC K1Z6A6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Clp R domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ACD_76C00029G0004 {ECO:0000313|EMBL:EKD33439.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD33439.1};
RN [1] {ECO:0000313|EMBL:EKD33439.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23019650; DOI=10.1126/science.1224041;
RA Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA Long P.E., Banfield J.F.;
RT "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT bacterial phyla.";
RL Science 337:1661-1665(2012).
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:EKD33439.1}.
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DR EMBL; AMFJ01033353; EKD33439.1; -; Genomic_DNA.
DR AlphaFoldDB; K1Z6A6; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 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; IPR001270; ClpA/B.
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; SSF81923; Double Clp-N motif; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 34..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 67..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 339..469
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 606..772
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 771..860
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
SQ SEQUENCE 866 AA; 96723 MW; 9ED991C40F16C35C CRC64;
MKGFVLNGKL YAFDELIDAS AIAMRHVRSA VSRIVTFFAL IIFAIVFVSF VYWVYQSGAE
TIFSKAFWFY PNTRAAHAFV IVIFACYIIY RAQKHAFVSI PVSKKSIDFT EPEISDFSYT
QSESYKSKVD ISKSFKLSAF HVFEQAFKIA SHLDNSEVKP MHIFAATLPS NEIMTIFFRL
GIKYNEIQEQ ISKRLGKIAS GSGTIFSDQA IEVALSSYIN AASHNRPYVS VIEVFIESYK
KDEFLKELLF DKGVDEEKLE NVAAWIRVRE QLRERYEKGR GRAMLKPTGA MNRAYTAVAT
PFLDSVSVDM TATAVRGQLP LLVGREKAVS EIFRIIEGGN QSVILVGNSG VGKDAIIEGI
AELMAEESVP KILQDKRLVK ISIPHLIAGA QSGQVEERIL RTMYDVARSG NIVLAVDDLD
QLPPEAHGAL SSELAKGYTF MIATSELRAY ASKIEQGVLG REFIKINIEE PEKNEAIRIL
ESKIGYIEYK HSVFFSFDAL EKCVTLADRY VHEKYLPEKA IELAKEAALL ASKRGKKAFV
LTTDVEKIVA EKTGIPQSQI GTDEREKLLN LEAEIHKRVI GQDEAIKAVS SALRRARTAL
KSKNRPIGTF LFLGPTGVGK TELAKATASV YFGSDDAMIR FDMSEYQEKG SVYRILGGPG
QEGLLTEAVR RKPFSLLLLD ELEKAHPDIL NLFLQVMDDG RLTDAQGRTV DFTNVILIAT
SNAGTEFIQQ SVKSNIPIEQ IKERLLDEGL KRVYRPEFLN RFDGIVVFKP LSEEEVVQIA
YLMIAKLSSD LEETRGIRLV AEDEAVYELA KKGYDPVFGA RPLRRVIQEE VNNSIATILL
QGGASRRDTI VLGNGGEIRV EKAQKL
//