ID   O83779_TREPA            Unreviewed;       809 AA.
AC   O83779;
DT   01-NOV-1998, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1998, sequence version 1.
DT   27-MAR-2024, entry version 142.
DE   SubName: Full=ATP-dependent Clp protease subunit A (ClpA) {ECO:0000313|EMBL:AAC65770.1};
GN   OrderedLocusNames=TP_0801 {ECO:0000313|EMBL:AAC65770.1};
OS   Treponema pallidum (strain Nichols).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC   Treponema.
OX   NCBI_TaxID=243276 {ECO:0000313|EMBL:AAC65770.1, ECO:0000313|Proteomes:UP000000811};
RN   [1] {ECO:0000313|EMBL:AAC65770.1, ECO:0000313|Proteomes:UP000000811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nichols {ECO:0000313|EMBL:AAC65770.1,
RC   ECO:0000313|Proteomes:UP000000811};
RX   PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA   Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G., Dodson R.,
RA   Gwinn M., Hickey E.K., Clayton R., Ketchum K.A., Sodergren E.,
RA   Hardham J.M., McLeod M.P., Salzberg S., Peterson J., Khalak H.,
RA   Richardson D., Howell J.K., Chidambaram M., Utterback T., McDonald L.,
RA   Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S., Hatch B.,
RA   Horst K., Roberts K., Watthey L., Weidman J., Smith H.O., Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL   Science 281:375-388(1998).
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; AE000520; AAC65770.1; -; Genomic_DNA.
DR   PIR; C71279; C71279.
DR   RefSeq; WP_010882246.1; NC_021490.2.
DR   AlphaFoldDB; O83779; -.
DR   STRING; 243276.TP_0801; -.
DR   EnsemblBacteria; AAC65770; AAC65770; TP_0801.
DR   GeneID; 57879320; -.
DR   KEGG; tpa:TP_0801; -.
DR   PATRIC; fig|243276.9.peg.787; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_2_12; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000000811; Chromosome.
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; 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:AAC65770.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:AAC65770.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000811};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          248..391
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          532..700
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          699..788
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   REGION          147..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   809 AA;  89328 MW;  D9C8CBEE250CAEEE CRC64;
     MKIIISASVQ IILDQAFDLA RKRRHEYITA EHVLFSALAH PAALEIINLC SADIALIHSN
     LSEFLKTQVP VDLSHTPSQS LGFQHLLKRA VLYCEANKKS ALEVGDLLVS LLQAETNYAS
     YYMRMSGMST ARLIEVIARV NGIRHGDKNV SMGSNAQERY SESDDVGESA GHGPPLDGTE
     GDGNTADVHV HYEHCAHKRT DADTHRYTVL EKYTVNLTER ARRGELAPLI GRTQEIERTI
     QILCRRQKNN PVHVGEAGVG KTAITEGLAQ RIVRCDVPEA LEGVEIFSLD MTSLLAGTKF
     RGDFEERLKR LAEELEKKTQ AILFIDEIHT VVGTGSGGSG GLDASNLLKP LLSSGKIRCI
     GSTTYEEYTK HFRKDQALAR RFQKIDIEEP SEEETLRILE GIRTLYEDFH AVHYSDEALA
     AAVRLSVQYI QGRHLPDKAI DIIDEAGACA KLSRGKHGTE GVCSVIGESD IDEIVAKIAK
     IPKQRVSASE IEKLRNFERS ISEKIFGQGE AIDLVTRTLK RARVGLRVKH KPIANLLFVG
     ATGVGKTELA RTLAQELGIV LHRFDMSEYQ EKHTVSRLIG SPPGYVGFEE GGLLTDAVRK
     QPHAVLLLDE IEKAHPDIFN VLLQVMDYAT LTDNQGRKAD FRNVILIMTS NAGARNMGVS
     LIGFHKGQVG TAVIDEAVER IFSPEFRNRL DAVIRFDALS LETMERIARK ELALVCEQLQ
     KKHIRFDITD DALALLAERS HSGGSGARNV ARLVEQEVAN VLADLMLFGG VAEGDALRCT
     VKDRHAQCNF LRIECVQSSY SGSIQDALG
//