ID K2FH05_9BACT Unreviewed; 842 AA.
AC K2FH05;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Clp R domain-containing protein {ECO:0000259|PROSITE:PS51903};
GN ORFNames=ACD_7C00096G0030 {ECO:0000313|EMBL:EKE21913.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:EKE21913.1};
RN [1] {ECO:0000313|EMBL:EKE21913.1}
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 -!- 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}.
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:EKE21913.1}.
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DR EMBL; AMFJ01002335; EKE21913.1; -; Genomic_DNA.
DR AlphaFoldDB; K2FH05; -.
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 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 7..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 446..499
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 842 AA; 94702 MW; 02719D522C037844 CRC64;
MIDNKIFEKF TIHAKSSLNE SLNIANYYGS DSICPEHLMF AIFLEKGSLG SNVLTDLHIK
KESFDKIFKF KNKNKKIIKN LELSPELKKN ITRAYLLASN FNYSYIGTEH LVFSIIEAPN
PMVTKILDIN AKNSSSSSAT SNKKLSDKIL NPHLKGKNIL DKSFLSGIFK ALNIPEADFP
AFSNNSTKNN STPNLDYFCN NLNAKVKNEE TLLIGREAEM ERIFNSLGRK SKNNPLLIGD
PGIGKTALIE GLAQRINSER VPQNLINKKI LALDIALVVA GTNFRGEFEQ RLKDILQEAA
TNKDTILFID EIHGIVGAGN ASGGLDAANI LKPLLTQGTI RCIGATTIEE YKKYIEKDSA
LERRFQPIML KEPSAKDSLK IIKGIRKNYE KFHNVDISDG ALAAAVDLSS RYIQDRFQPD
KSIDLIDETS SRIKNKHNVS PAIKELRMAE KKLDSLIEQK NFLIAEEKYD EAIALRKKEE
LLLEKISQLK NKQQKFEKDN KLVIEPEDIA QTISLGTNIP VQKILAQSSD RSKNIFDKLN
HIVIGQPEAL KKISQAILRA QSGIGDTEKP IGSFLFLGPS GVGKTLCAKT LAQEFFGDTP
SSLIKIDMSE FAEKHNVSRL IGAPAGYIGY GEGGKLTEKV RRQPYSLILF DEIEKAHPDV
FNILLQLLEE GILTDAEGRK VNFKNTIIIL TSNIGTKEFT RATSIGFSSR ENKNQMEKKF
AHIKRKVLAE LKEKIKPEIL NRLDEIIVFD ALNKKDIEEI VALELKKLSL RLYTERKIKL
TYSKNLVKFI IDKSFSTEKG ARYIKKNIRD FVENEIADKI TYAQIKNNAL KLDVKDKKIS
SH
//
