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Database: UniProt
Entry: D3SMC2_THEAH
LinkDB: D3SMC2_THEAH
Original site: D3SMC2_THEAH 
ID   D3SMC2_THEAH            Unreviewed;       984 AA.
AC   D3SMC2;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=ATPase AAA-2 domain protein {ECO:0000313|EMBL:ADC89902.1};
GN   OrderedLocusNames=Thal_1270 {ECO:0000313|EMBL:ADC89902.1};
OS   Thermocrinis albus (strain DSM 14484 / JCM 11386 / HI 11/12).
OC   Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Thermocrinis.
OX   NCBI_TaxID=638303 {ECO:0000313|EMBL:ADC89902.1, ECO:0000313|Proteomes:UP000002043};
RN   [1] {ECO:0000313|Proteomes:UP000002043}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14484 / JCM 11386 / HI 11/12
RC   {ECO:0000313|Proteomes:UP000002043};
RX   DOI=10.4056/sigs.761490;
RA   Wirth R., Sikorski J., Brambilla E., Misra M., Lapidus A., Copeland A.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C.,
RA   Tapia R., Bruce D., Goodwin L., Pitluck S., Pati A., Anderson I.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Chen A., Palaniappan K.,
RA   Bilek Y., Hader T., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Tindall B.J., Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Thermocrinis albus type strain (HI 11/12T).";
RL   Stand. Genomic Sci. 2:194-202(2010).
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; CP001931; ADC89902.1; -; Genomic_DNA.
DR   RefSeq; WP_012992308.1; NC_013894.1.
DR   AlphaFoldDB; D3SMC2; -.
DR   STRING; 638303.Thal_1270; -.
DR   KEGG; tal:Thal_1270; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_2_0; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000002043; 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   Gene3D; 4.10.860.10; UVR domain; 1.
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; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF193; CHAPERONE PROTEIN CLPB; 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.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002043};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..72
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          94..161
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          543..650
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   984 AA;  112369 MW;  D9D3CAD953BDB126 CRC64;
     MFSENLFSAR ALQYVEKAKE LAVQEKDTKV DTDHLLLAFL SDEKSPLFKY LEKRGVPAKE
     FASRVKEYLR KVKTQLEKAV DQEAKHLIDL RSKIMQVKSD IGQLQLEVDK VKRAQERLQR
     ELQQAKRYGD YWTAQELQVE LSRLERLYSQ YKSQLESVER SLSSVFKQED VRAFMENRLS
     IDGLVRKALE ESPILEQVKE LGFSPERFTE AVARKVFGKE PTLDYSQYLL KVLEKAQDKA
     ISEGSPQVEP YHLASALIEA VDTVGGKLIN EVTGGDKMKD TTQELREEEK SPLERFGVNM
     TQLAREGKLD PVIGREKEIN QVIEVLLRRT KNNPVLVGDP GVGKTAIVEG LAQRIANKEV
     PTELQDKELW SIDMASLLAG SKYRGEFEER LKALIDEVKQ KGNVILFIDE VHTVVGAGKA
     EGAVDASNIL KPALARGEIR LIGATTVDEY RKYIEKDPAL ERRFQPIYVD EPTEEQTIEI
     LKGLRTKLEN HHKVKISDEA IEAAVKLTRR YVTFRKLPDK AIDALDQACA RKKLSVVAVP
     PEVQELDRRI KALDEEIQKA FLEGNYEKEA QLKIKKVQLE KERQQLLEKT GGTDARIKEI
     KRRMEELDTE IIRAAEKGDY EREAQLKIEK VKLEKELKEL ELKKSEALVV TWDDVAAVVS
     EWTGIPVQRL KEEEMERLLK LEEELHRRVI DQEHAVRAVA EAIRRARAGL KDPKRPIASF
     LFLGPTGVGK TELSKALAEL LFGDEDALIR LDMSEFKEEH SIAKLIGAPP GYVGYEEGGK
     LTEAVRRKPY SVLLLDEVEK AHPRVFDLFL QVLDDGRLTD SHGRTVDFRN TVIIMTSNIG
     SQYLLSLSLD GDEEKVQREF EKAKEKVLEE LKYHFRPEFL NRIDEIVVFK PLTMKELLQI
     VDLLVASISR RLEDRGIKIE LTQAAKEQLA RMGYDPAYGA RPLRRTLQRY IETPLADKII
     RGEVKDGQKV LVDYRDGQVV VEAV
//
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