ID A0A0G0BQF5_9BACT Unreviewed; 851 AA.
AC A0A0G0BQF5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Negative regulator of genetic competence ClpC/mecB {ECO:0000313|EMBL:KKP33317.1};
GN ORFNames=UR22_C0001G0130 {ECO:0000313|EMBL:KKP33317.1};
OS Parcubacteria group bacterium GW2011_GWC2_32_10.
OC Bacteria.
OX NCBI_TaxID=1618918 {ECO:0000313|EMBL:KKP33317.1, ECO:0000313|Proteomes:UP000034155};
RN [1] {ECO:0000313|EMBL:KKP33317.1, ECO:0000313|Proteomes:UP000034155}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKP33317.1}.
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DR EMBL; LBOJ01000001; KKP33317.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0BQF5; -.
DR STRING; 1618918.UR22_C0001G0130; -.
DR PATRIC; fig|1618918.3.peg.131; -.
DR Proteomes; UP000034155; Unassembled WGS sequence.
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 78, MITOCHONDRIAL; 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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 59..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 314..458
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 591..736
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 758..843
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
SQ SEQUENCE 851 AA; 96708 MW; CB61EDA0329B093E CRC64;
MKFDLKNSEI FSLVKIQKIF KLEYLNFLKN LFLCLFIISV FVFSISYYEI LTLSTTLKAP
VIFLALFLLF FEFSLFIKLK KINSKLLVNL KDAILNPDEY NLAEFLNIES AKFIQNAIRF
CNNKKIFQIN STALLYSAVK YSKEINILCF RLGIDTNKLL INVKNFLEKS LTDGSSIEAF
SEDFKSVILS AGKIAVERNH LRITEKEILI ALAQNDKFFQ KVLIDYDLKE KDVENLSLWL
DSVEERVRSQ KIFWSSDNLS RAGSNGQDWA FGYTITLDQY SVDWRDTVSK WLYKEVVGHK
KEIEETEMIL ARSNLSNVLI IGDPGTGRKS IIEAVAQKCF LSQSLPELNN KRVVELDMIA
LLSSIQDSEK LETILDKIFQ EAFSAGNVIL VIDELQNYVG QKIAKAGAFD ISGILTKYLA
IPTFQFVGIT SFAGLHQNIE QNPSFLEYFR KIEVSEITEI ETIKILQNLA LELEAKYKIL
VIYPAIREIV NLTGRYFPST PFPKKAIDVL DEAVVYAQTL KEKVVMPHHI AKIISDKTQI
PVGKMEFKEK EVLLNLENLI HQRIVNQEEA VSEISIAMRR ARAGIASKKR PMGTFLFMGP
TGVGKTETAK ALAQIYFGGE DKTIRIDMSE FQSLSDIPRL IGAISPVEMQ GLLTTPVRES
PFSLVLLDEI EKAHFNILNL FLQVLDEGHI TDGQGRKVMF TNTIIICTSN AGASDIFKSV
EAGEKLDKEK ILLGLFEKNI FRPEFVNRFD ATVIFHPLTK DNLLKIAQIT LVSLQKNLKE
KEIDFIITES LKAKIVELSY KPEFGAREMR RVVQDKVENS IAEALISDKL AKGNKFEINP
ETFEIIVNPV E
//