ID Q9F879_BRAJP Unreviewed; 802 AA.
AC Q9F879;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 13-SEP-2023, entry version 102.
DE SubName: Full=ClpA-like protein {ECO:0000313|EMBL:AAG17282.1};
OS Bradyrhizobium japonicum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=375 {ECO:0000313|EMBL:AAG17282.1};
RN [1] {ECO:0000313|EMBL:AAG17282.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA 110 {ECO:0000313|EMBL:AAG17282.1};
RX PubMed=11157281; DOI=10.1128/AEM.67.2.1011-1014.2001;
RA Louch H.A., Miller K.J.;
RT "Synthesis of a low-molecular-weight form of exopolysaccharide by
RT Bradyrhizobium japonicum USDA 110.";
RL Appl. Environ. Microbiol. 67:1011-1014(2001).
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; AF254897; AAG17282.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9F879; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0043335; P:protein unfolding; 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; IPR004176; Clp_R_dom.
DR InterPro; IPR013461; ClpA.
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 NCBIfam; TIGR02639; ClpA; 1.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF111; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPA; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 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.
DR PROSITE; PS51903; CLP_R; 1.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..148
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 150..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 802 AA; 88253 MW; CB1E8FB6B353D9AC CRC64;
MPTFSQSLEQ SLHRALAIAN ERHHQYATLE HLLLSLIDDS DAAAVMRACS VDLDKLRTSL
VNYLETEFEN LVTDGADDAK PTGGFQRVIQ RAVIHVQSSG REEVTGANVL IAIFAERESH
AAYFLQEQDM TRYDAVNYIS HGIAKRPGVS EARPVRGVDE ETETKGSDDA KKKGEALETY
CVNLNKKARD GKIDPVIGRN SEINRAIQVL CRRQKNNPLF VGEAGVGKTA IAEGLAKRIV
DSEVPEVLAA ATVFSLDMGT LLAGTRYRGD FEERLKQVLK ELEAHPNAIL FIDEIHTVIG
AGATSGGAMD ASNLLKPALA SGTIRCMGST TYKEYRQHFE KDRALVRRFQ KIDINEPTVE
DAIAILKGLK PYFEDYHRLK YTNEAIEAAV QLSSRYIHDR KLPDKAIDVI DESGAAQMLV
AENKRKKTIG IKEIETTIAS MARIPPKSVS KDDAEVLKHL EQTLKRTVFG QDKAIESLAA
SIKLARAGLR EPEKPIGCYL FSGPTGVGKT EVAKQLAASL GVELLRFDMS EYMERHTVSR
LIGAPPGYVG FDQGGLLTDG VDQHPHCVVL LDEIEKAHPD LYNVLLQIMD HGRLTDHNGK
QVNFRNVILI MTTNAGASDL AKQAFGFTRS KREGDDHDAI NRQFAPEFRN RLDAIVSFSH
LSVEVIGTVV EKFVLQLEAQ LGDRDVTIEL SEPAKAWLVQ HGYDEQMGAR PMARVIQEHI
KKPLADEVLF GKLKSGGHVR VVLVKDEADE TKEKIGFEFV EGPVTPKQEK LPGARKRPPG
KPKPGGPGGS KGPTSKGPLV KA
//