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Database: UniProt
Entry: A0A074M7V0_ERYLO
LinkDB: A0A074M7V0_ERYLO
Original site: A0A074M7V0_ERYLO 
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}.
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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
//
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