ID A0A109JDB4_9BRAD Unreviewed; 798 AA.
AC A0A109JDB4;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:KWV46812.1};
GN Name=clpA {ECO:0000313|EMBL:KWV46812.1};
GN ORFNames=AS156_20460 {ECO:0000313|EMBL:KWV46812.1};
OS Bradyrhizobium macuxiense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1755647 {ECO:0000313|EMBL:KWV46812.1, ECO:0000313|Proteomes:UP000057737};
RN [1] {ECO:0000313|EMBL:KWV46812.1, ECO:0000313|Proteomes:UP000057737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BR 10303 {ECO:0000313|EMBL:KWV46812.1,
RC ECO:0000313|Proteomes:UP000057737};
RA Zelli J.E., Simoes-Araujo J.L., Barauna A.C., Silva K.;
RT "Draft Genome Sequence of the Strain BR 10303 (Bradyrhizobium sp.) isolated
RT from nodules of Centrolobium paraense.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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:KWV46812.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LNCU01000115; KWV46812.1; -; Genomic_DNA.
DR RefSeq; WP_066513865.1; NZ_LNCU01000115.1.
DR AlphaFoldDB; A0A109JDB4; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000057737; Unassembled WGS sequence.
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:0043335; P:protein unfolding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000313|EMBL:KWV46812.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:KWV46812.1};
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 755..798
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 798 AA; 87878 MW; 77AE09CFD932A4E9 CRC64;
MPTFSQSLEQ SLHRALAIAN ERHHQYATLE HLLLSLIDDS DAAAVMRACS VDLDKLRTSL
VNYLETEFEN LVTDGADDAK PTAGFQRVIQ RAVIHVQSSG REEVTGANVL IAIFAERESH
AAYFLQEQDM TRYDAVNYIS HGIAKRPGVS EARPVRGVDE ETETKGNEDA KKKGEALETY
CVNLNKKARD GKIDPVIGRN AEINRAIQVL CRRQKNNPLF VGEAGVGKTA IAEGLAKRIV
DSDVPEVLAA ATVFSLDMGT LLAGTRYRGD FEERLKQVLK ELEAHPNAIL FIDEIHTVIG
AGATSGGAMD ASNLLKPALA SGTIRCMGST TYKEYRQHFE KDRALVRRFQ KIDVNEPTVE
DAIAILKGLK PYFEDYHRLK YTNEAIEAAV QLSSRYIHDR KLPDKAIDVI DESGAAQMLV
AENKRKKTIG IKEIETTIAT MARIPPKSVS KDDAEVLKHL EQTLKRVVFG QDKAIESLSA
SIKLARAGLR EPEKPIGCYL FSGPTGVGKT EVAKQLAASL GVELLRFDMS EYMERHTVSR
LIGAPPGYVG FDQGGLLTDG VDQHPHCVVL LDEIEKAHPD LYNVLLQIMD HGRLTDHNGK
QVNFRNVILI MTTNAGAADL ARQAFGFTRS KREGDDHEAI SRQFAPEFRN RLDAIVSFAH
LNADVIGMVV EKFVLQLEAQ LADRDVTIEL SEPAKAWLIE HGYDEQMGAR PMARVIQEHI
KKPLADEVLF GQLKGGGHVR VVLVKDEQEK DKIGFEFVEG PVTPKPENLP ARKRKPKSGG
GGGGGTKAPP SRGPLVKA
//
