ID H8GSD3_DEIGI Unreviewed; 746 AA.
AC H8GSD3;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE SubName: Full=ATPase AAA-2 {ECO:0000313|EMBL:AFD25206.1};
GN Name=clpA {ECO:0000313|EMBL:AFD25206.1};
GN OrderedLocusNames=DGo_CA1279 {ECO:0000313|EMBL:AFD25206.1};
OS Deinococcus gobiensis (strain DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=745776 {ECO:0000313|EMBL:AFD25206.1, ECO:0000313|Proteomes:UP000007575};
RN [1] {ECO:0000313|EMBL:AFD25206.1, ECO:0000313|Proteomes:UP000007575}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0
RC {ECO:0000313|Proteomes:UP000007575};
RX PubMed=22470573; DOI=10.1371/journal.pone.0034458;
RA Yuan M., Chen M., Zhang W., Lu W., Wang J., Yang M., Zhao P., Tang R.,
RA Li X., Hao Y., Zhou Z., Zhan Y., Yu H., Teng C., Yan Y., Ping S., Wang Y.,
RA Lin M.;
RT "Genome sequence and transcriptome analysis of the radioresistant bacterium
RT Deinococcus gobiensis: insights into the extreme environmental
RT adaptations.";
RL PLoS ONE 7:E34458-E34458(2012).
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DR EMBL; CP002191; AFD25206.1; -; Genomic_DNA.
DR RefSeq; WP_014684689.1; NC_017790.1.
DR AlphaFoldDB; H8GSD3; -.
DR STRING; 745776.DGo_CA1279; -.
DR KEGG; dgo:DGo_CA1279; -.
DR PATRIC; fig|745776.4.peg.1317; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_0; -.
DR OMA; GRVIQEH; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000007575; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; 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; IPR001270; ClpA/B.
DR InterPro; IPR018368; ClpA/B_CS1.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
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; 2.
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.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..64
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
SQ SEQUENCE 746 AA; 78884 MW; 9338EE4CD6391ECA CRC64;
MIGEHLQVTI GRAADYARVA GHEYVTLEHL LLALTHDPEA LETLLALGVD VEALRETLNA
ELQEASASGE ALPEDDDPDF TLGVHRVVEG AVLQLHASGK GSEEADGARV LAELLEEEDS
PARAALEAQG VTRLDVLSYL SHGVAKVGGR SRERRVAGVD GAAAEAEAPA ETDPLEAYAT
DLTAAARAGE FDPVIGRDAE LERTVHILAR RGKNNPVLVG EPGVGKTALA EGLAQRVVGG
QAPGFLKDAS VYALNLGALL AGTRYRGDFE ARLGAVVAAL DGRNAVLFID ELHTIVGAGA
TEGGSVDAAN LLKPALARGR LRVLGATTPA ELRHLEKDRA LWRRFQTVEV PEPSEEDALA
ILRGLAPHYA AHHGVTYADD ALDAAVRLSA RHLRDRFLPD KAIDVLDEAG AARRSAGKGG
EIGVPDIEAT VARMARVPLG AVKAEEVRSL ATLEADLGAR VFGQEKAVGA VAAAVKLARA
GLRDPQKPQG MFLFAGPTGV GKTELARALA ERLGIHLARF DMSEYQEPHT VARLIGAPPG
YVGFDQGGLL TDAVAKHPHA VLLLDEIEKA HPDVYNVFLQ LMDHGTLTDH AGKKVDGRGL
LLIFTTNAGA ADASRPALGF SRVGRAGEES AAVTRTFTPE FRNRLDAVIH FAPLSPEVMT
GVVDKFLRAL EAQLAERRVA LTVTPAARAR LAQLGYDPAL GARPLARVIE ERLGRPLADE
LLFGRLTGGG TVMVDTDDEG GFRFSP
//