ID A0A3D9BWR3_9RHOB Unreviewed; 775 AA.
AC A0A3D9BWR3;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:REC57965.1};
GN Name=clpA {ECO:0000313|EMBL:REC57965.1};
GN ORFNames=DRV84_05115 {ECO:0000313|EMBL:REC57965.1};
OS Rhodosalinus sediminis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodosalinus.
OX NCBI_TaxID=1940533 {ECO:0000313|EMBL:REC57965.1, ECO:0000313|Proteomes:UP000257131};
RN [1] {ECO:0000313|EMBL:REC57965.1, ECO:0000313|Proteomes:UP000257131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WDN1C137 {ECO:0000313|EMBL:REC57965.1,
RC ECO:0000313|Proteomes:UP000257131};
RX PubMed=29043957; DOI=10.1099/ijsem.0.002424;
RA Guo L.Y., Ling S.K., Li C.M., Chen G.J., Du Z.J.;
RT "Rhodosalinus sediminis gen. nov., sp. nov., isolated from marine
RT saltern.";
RL Int. J. Syst. Evol. Microbiol. 67:5108-5113(2017).
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:REC57965.1}.
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; QOHR01000004; REC57965.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D9BWR3; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000257131; 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:REC57965.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:REC57965.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000257131};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 150..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 775 AA; 84749 MW; 7EA25A8D3E509048 CRC64;
MPSFSTTLEQ AIHSALALAN SRSHEFATLE HLLLALVDEP EASKVLKACN VDTEELRGTL
VDFIDEELAN LVTDVEGSEA VPTTAFQRVI QRAAIHVQSS GRTEVTGANV LVAIFAERES
NAAFFLQEQD MTRYDAVNFI AHGVAKNPAY GESRPVTGAS EQQEEEAQAA SEPADQKESA
LGKYCVDLNA KAREGDVDPL IGRDTEVERC IQVLCRRRKN NPLLVGDPGV GKTAIAEGLA
RKIVKGETPE VLKGTTIYAL DMGALLAGTR YRGDFEERLK AVVQELEEHQ DGVLFIDEIH
TVIGAGATSG GAMDASNLLK PALQGGKLRT MGSTTYKEFR QHFEKDRALS RRFQKIDVTE
PTVDDAVKIL KGLKPYFEKH HAVKYTTDAI KTAVELSARY ITDRKLPDKA IDVIDEAGAA
QHLVAESKRR KTIGQKEIEG VVAKIARIPP KNVSKDDAEV LKDLEGTLKR VVFGQDTAIE
ALSSSIKLAR AGLREPDKPI GNYLFAGPTG VGKTEVAKQL ADTLGVELLR FDMSEYMEKH
AVSRLIGAPP GYVGFDQGGL LTDGVDQHPH CVLLLDEIEK AHPDVFNVLL QVMDHGTLTD
HNGRQVDFRN VILIMTSNAG AIEQAQAAVG FGRDRREGED QAAIERTFTP EFRNRLDAVI
SFGALPKEVI LQVVEKFVLQ LEAQLMDRNV TIELTESAAE WLAERGYDDK MGARPLGRVI
QENIKKPLAE ELLFGKLAKG GVVRVAVKDG ELDLQIESTP KPRLSSKKPP LLTAD
//