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Database: UniProt
Entry: K1Z2T7_9BACT
LinkDB: K1Z2T7_9BACT
Original site: K1Z2T7_9BACT 
ID   K1Z2T7_9BACT            Unreviewed;       523 AA.
AC   K1Z2T7;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=ATP-dependent Clp protease ATPase subunit {ECO:0000313|EMBL:EKD43812.1};
DE   Flags: Fragment;
GN   ORFNames=ACD_72C00108G0008 {ECO:0000313|EMBL:EKD43812.1};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD43812.1};
RN   [1] {ECO:0000313|EMBL:EKD43812.1}
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:EKD43812.1}.
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DR   EMBL; AMFJ01029087; EKD43812.1; -; Genomic_DNA.
DR   AlphaFoldDB; K1Z2T7; -.
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; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 2.
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; 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; 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; 1.
DR   SMART; SM01086; ClpB_D2-small; 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   Hydrolase {ECO:0000313|EMBL:EKD43812.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protease {ECO:0000313|EMBL:EKD43812.1}.
FT   DOMAIN          267..409
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          434..522
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EKD43812.1"
SQ   SEQUENCE   523 AA;  57438 MW;  C8FB5DD422B320AA CRC64;
     VGKNSIIAGL AQKMVEDDVP ARLQDKRLVR LSVPKLLAGT TPAGAVERLI GIMQDIGRSG
     NVILFINNIH ELTGVSAGGE SGSLDVAGTL NEYLGSGRFL TFATTTQDEY SRHIVGSPLS
     NLFAKVEIKE MDENQAIQVL ESKVGNIEYK QNVFFSYDAV AKSVQLAMRF LHESYLPGSA
     QELMTEAASY ARSKKGLNSF VTGEEVAAIV AQKTGVPVNT VSADESTKLM HLEEEMHKRV
     IGQVEAVDLV ANALRRARAE IRSSKRPIAN FLFLGPTGVG KTELAKTIAE IYFGGEERMV
     RLDMSEYQDK SSIYRLIGTP GEKGSGMLTE AIRRSPFSLL LLDEMEKADK DILNLFLQVM
     DDGRLTDSVG RVVDFTNVIL IATANAGTAY VQEQLRAGVT SEIIKDKLLH GELKQYFRPE
     FLNRFDGIVL FKALNREDII KIAGLMLKRV ASDLEAKGIE LKIEPAAMEF LADVGFDPEF
     GARPMRRALQ EKVENQLAEL LISGKLKRRD TVVIGQGGEI KIV
//
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