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Database: UniProt
Entry: F4LP75_TREBD
LinkDB: F4LP75_TREBD
Original site: F4LP75_TREBD 
ID   F4LP75_TREBD            Unreviewed;       863 AA.
AC   F4LP75;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 66.
DE   SubName: Full=ATP-dependent Clp protease, ATP-binding subunit clpA {ECO:0000313|EMBL:AEE15951.1};
GN   OrderedLocusNames=Trebr_0508 {ECO:0000313|EMBL:AEE15951.1};
OS   Treponema brennaborense (strain DSM 12168 / CIP 105900 / DD5/3).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC   Treponema.
OX   NCBI_TaxID=906968 {ECO:0000313|EMBL:AEE15951.1, ECO:0000313|Proteomes:UP000006546};
RN   [1] {ECO:0000313|Proteomes:UP000006546}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12168 / CIP 105900 / DD5/3
RC   {ECO:0000313|Proteomes:UP000006546};
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Pagani I.,
RA   Teshima H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S.,
RA   Wellnitz S., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Treponema brennaborense DSM 12168.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; CP002696; AEE15951.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4LP75; -.
DR   STRING; 906968.Trebr_0508; -.
DR   KEGG; tbe:Trebr_0508; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_2_12; -.
DR   OMA; GRVIQEH; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000006546; 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; 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:AEE15951.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:AEE15951.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006546};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..141
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          176..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..198
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   863 AA;  92351 MW;  A2AEFC3B0EFE5524 CRC64;
     MKITPQLQKI INSAMEDAGK SGHEFVTPEH LLYASLKFPP VRDLLLVCGG DVDTILTNVN
     SYLETKVPVA KDHTPIQTVG FQNVIERAVL HCVAAEKQEL EITDVIVSML DEPKNYCSYY
     LHKGGIDRLR LIEVISYIKY KCDESADLQS CIAAMLEDEQ FRDGVTDAFP VRSVGASEKP
     SADSAKSAAG TSASSAGDGA ESAEGGGAGK SARRTALERY AVDLIAEAKN GNLESFIGRD
     AELERTVQVL CRRSKNNPIH VGDAGVGKTA ITHGLAARIA ADQVPDALAG YALYSLDMGA
     LIAGTKFRGD FEDRFKRIID ELLKKEKAIL FIDEIHTIIG AGASGSGNLD ASNLLKPVLT
     SGKIRCIGST TFEEYARIFE KDRALARRFQ KIDILEPGAA DTVKILEGLK PAYEAYHGVS
     YTAPALAAAV DLSVQYLPDR RLPDKAIDIL DEAGAYVRIH RKAANRPRTV SAAAAAGGSG
     TVSSAAFSAG AAFSHGAAVP RPQRKPRVTV ALVEKIVSKM ARIPERSVKT DERDVLRNLE
     SVLEREIFGQ DEAVSLVVQA VKRSRAGLRD PDKTAANFLF AGPTGVGKTE LARALAQSLG
     MPLLRFDMSE YQEKHTVSRL IGSPPGYVGF EEGGLLTDAV RKEPYAVVLL DEIEKAHADI
     YNILLQVMDY GQLTDNQGRK ADFRNAILIM TSNAGARDIG KPLIGFGGRA ADGSAVREAV
     EKAFTPEFRN RLDAVVPFGH LDRLVAEDIV RKELRKLAAR LARKKVSLEV DDACVAFLAD
     RGYSREFGAR NVARTVDSLV ASALVDAVLF GKLADGGTVR CSVSGGAQTA VGGVQSAGTS
     GAGNTAAPAD VSGAERSVTF TYA
//
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