ID A0A074M7V0_ERYLO Unreviewed; 801 AA.
AC A0A074M7V0;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Clp protease ClpX {ECO:0000313|EMBL:KEO89489.1};
GN Name=clpA {ECO:0000313|EMBL:KEO89489.1};
GN ORFNames=EH31_12650 {ECO:0000313|EMBL:KEO89489.1};
OS Erythrobacter longus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=1044 {ECO:0000313|EMBL:KEO89489.1, ECO:0000313|Proteomes:UP000027647};
RN [1] {ECO:0000313|EMBL:KEO89489.1, ECO:0000313|Proteomes:UP000027647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6997 {ECO:0000313|EMBL:KEO89489.1,
RC ECO:0000313|Proteomes:UP000027647};
RA Zheng Q.;
RT "A comprehensive comparison of genomes of Erythrobacter spp. strains.";
RL Submitted (APR-2014) 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:KEO89489.1}.
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; JMIW01000005; KEO89489.1; -; Genomic_DNA.
DR RefSeq; WP_034960625.1; NZ_JMIW01000005.1.
DR AlphaFoldDB; A0A074M7V0; -.
DR STRING; 1044.EH31_12650; -.
DR eggNOG; COG0542; Bacteria.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000027647; 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:KEO89489.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:KEO89489.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027647};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 145..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..801
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 801 AA; 87737 MW; B74FA306F697AA4C CRC64;
MPSFAQNLER TLHNALAHAS ERRHEYATLE HLLLALIDDE DGAAVMGACG VDLAELGEVV
KQYLDQEYQS LKTEEDADPQ PTAGFQRVIQ RAILHVQSSG KDTVTGANVL VALFSERDSY
AVYFLQQQDM SRLDAVSYIS HGIGKGGRQI ESSNASGSDD SAPNDAEAAK DSGNKKETAL
DQFTVNLNKK AQDGKVDPLI GRGPEVDRTV QILCRRSKNN PLYVGDPGVG KTAIAEGLAR
KIVEGDVPEV LAPAVIYSLD MGALLAGTRY RGDFEERLKQ VVSELEGMPD AVLFIDEIHT
VIGAGATSGG AMDASNLLKP ALSGGTIRCI GSTTYKEFRN HFEKDRALLR RFQKIDVNEP
TIEDTVKILK GLRSAFEDHH NVKYTPDALK TAVELSARYI NDRKLPDKAI DVIDEVGAMQ
MLLPPSRRKK KITAREIEQV IATMARIPPK SVSKDDKKAL ENLDRDLKHV VFGQDEAISR
LATAMKLSRA GLRDPDKPIG SFLFSGPTGV GKTEVARQLS SIMGIELKRF DMSEYMERHS
VSRLIGAPPG YVGYDQGGLL TDAVDQNPHC VLLLDEIEKA HPDLFNILLQ VMDNGRLTDH
HGKTVDFRNV VLIMTTNAGA ADMAKSGIGF GDVSKEDAGT EAVNKMFTPE FRNRLDAIVP
FAYLGRDTVA RVVDKFILQL ELQLAEQNVD IQFDSDARAW LAAKGYDRLY GARPMGRLIQ
DKIKQPLAEE LLFGKLAEGG EVSVTMKDGK PAFELTPAAP KEKPKPKPRR KPAAKKTPAA
KKDDSQEDKS KPEASDSDKE G
//