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Database: UniProt
Entry: G2FE62_9GAMM
LinkDB: G2FE62_9GAMM
Original site: G2FE62_9GAMM 
ID   G2FE62_9GAMM            Unreviewed;       593 AA.
AC   G2FE62;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:EGW54832.1};
GN   Name=clpA1 {ECO:0000313|EMBL:EGW54832.1};
GN   ORFNames=TevJSym_ah00100 {ECO:0000313|EMBL:EGW54832.1};
OS   endosymbiont of Tevnia jerichonana (vent Tica).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX   NCBI_TaxID=1049564 {ECO:0000313|EMBL:EGW54832.1, ECO:0000313|Proteomes:UP000005167};
RN   [1] {ECO:0000313|EMBL:EGW54832.1, ECO:0000313|Proteomes:UP000005167}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Gardebrecht A., Markert S., Felbeck H., Thuermer A., Albrecht D.,
RA   Wollherr A., Kabisch J., Lehmann R., Daniel R., Liesegang H., Hecker M.,
RA   Sievert S.M., Schweder T.;
RT   "The endosymbionts of the deep-sea tubeworms Riftia pachyptila and Tevnia
RT   jerichonana share an identical physiology as revealed by proteogenomic
RT   analyses.";
RL   ISME J. 0:0-0(2011).
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:EGW54832.1}.
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DR   EMBL; AFZB01000008; EGW54832.1; -; Genomic_DNA.
DR   AlphaFoldDB; G2FE62; -.
DR   PATRIC; fig|1049564.3.peg.1194; -.
DR   eggNOG; COG0542; Bacteria.
DR   Proteomes; UP000005167; 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: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; -; 1.
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; 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: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   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 2.
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|RuleBase:RU004432};
KW   Hydrolase {ECO:0000313|EMBL:EGW54832.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:EGW54832.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005167};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..144
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          145..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   593 AA;  65724 MW;  CC833DDA67916633 CRC64;
     MLSKELEFTL NQAFIRAKEK RHEFITVDHL LLALLENPAA CEVLRACDAD LEQLREEISA
     FVDGSTPLIP EGEERDTQPT LGFQRVLQRA VFHVQSSGKK EVSGANVLVA LFSEQDSQAL
     FFLDQQDITR LDVINYISHG LSKQDEEEHD DSLDLTEQPQ ADSQPSALET YATNLNKLAE
     AGKIDPLIGR RAEIERTIQI LCRRRKNNPL LVGEAGVGKT AIAEGLAKMI VEEQVPEVLA
     DATIYALDLG SLVAGTKYRG DFEKRLKAVL AEFRKQPDSI LFIDEIHTII GAGSASGGVM
     DASNLIKPVL ASGELRCIGS TTYQEFRGIF EKDRALARRF QKIDVEEPSV EETVEILKGL
     KSRFEEHHEI EYTQGALQSA ATLSEKYIND RHLPDKAIDV IDEAGANVHL QPPEERKKLI
     GVDEIEAIVA KIARIPPKKV SASDTEALRN LSRDLQMVVY GQDDAIEALT AAIRMNRSGL
     LREGRPVGSF LFAGPTGVGK TEVTRQLARI MGMELIRFDM SEYMERHAVS RLIGAPPGYV
     GFDQGGLLTE EINKHPHSVL LLDEIEKAHP GYLQPAVAGD GPRYPDRQQW PQS
//
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