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Database: UniProt
Entry: Q5FTA9_GLUOX
LinkDB: Q5FTA9_GLUOX
Original site: Q5FTA9_GLUOX 
ID   Q5FTA9_GLUOX            Unreviewed;       771 AA.
AC   Q5FTA9;
DT   01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2005, sequence version 1.
DT   24-JAN-2024, entry version 113.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:AAW60387.1};
GN   OrderedLocusNames=GOX0609 {ECO:0000313|EMBL:AAW60387.1};
OS   Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=290633 {ECO:0000313|EMBL:AAW60387.1, ECO:0000313|Proteomes:UP000006375};
RN   [1] {ECO:0000313|EMBL:AAW60387.1, ECO:0000313|Proteomes:UP000006375}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=621H {ECO:0000313|EMBL:AAW60387.1,
RC   ECO:0000313|Proteomes:UP000006375};
RX   PubMed=15665824; DOI=10.1038/nbt1062;
RA   Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA   Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT   "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT   oxydans.";
RL   Nat. Biotechnol. 23:195-200(2005).
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; CP000009; AAW60387.1; -; Genomic_DNA.
DR   RefSeq; WP_011252186.1; NZ_LT900338.1.
DR   AlphaFoldDB; Q5FTA9; -.
DR   STRING; 290633.GOX0609; -.
DR   KEGG; gox:GOX0609; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_2_5; -.
DR   OMA; GRVIQEH; -.
DR   Proteomes; UP000006375; 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:AAW60387.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:AAW60387.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006375};
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..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..172
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   771 AA;  85138 MW;  7794C79F635E3038 CRC64;
     MLSRTLEQTL HRALTFAGDR RHEYATLEHL LLALTEDDDA LTVFRACGID LDKLRSDLTD
     FLDKDLAGLA AERPTEPKPT AAFQRVIQRA AIHVQSTGRD EVTGANVLVA LFAERESHAV
     YFLQLQDMTR LDAVNFISHG IAKAPDRGAG RRPAAASKDT SEREERKESA KEGALATYCV
     DLNERAREGR IDPLIGRDQE IERTIQILCR RTKNNPLYVG DPGVGKTAIA EGLAKRIVEG
     DVPEVLLNST IYSLDMGSLL AGTRYRGDFE ERLKAVVTEM DQTPGAILFI DEIHTVIGAG
     ATSGGAMDAS NLLKPALAAG TLRCIGSTTY KEFRQHFEKD RALVRRFQKI DVPEPSIEDA
     VKILRGLKGS YEKHHKVRYT DEALRGAVEL AAKYVHDRKL PDKAIDVIDE VGAARMLVPE
     NKRRKTVTLK DVEEAIAKIA RIPPKSVSAD DRETLRHLER DLRNMVFGQD KAIDALAAAI
     KLSRAGLRDA EKPIGNYLFS GPTGVGKTEV AKQLANSLGI ELIRFDMSEY MERHSISRLI
     GAPPGYVGFD QGGLLTDAID QHPHAVLLLD EIEKAHPDLF NVLLQVMDHG RLTDHNGKVV
     DFRNVILIMT TNAGAADLSK ETIGFGRTVR SGEDEEAIKR LFTPEFRNRL DAIIPFANLT
     PETVGRVVEK FVLQLEAQLA DRHVTIEISS SAKEWLAERG YDRLYGARPL GRVIQEHIKK
     PLAEELLFGR LAQGGAVKIG MKNGALDFDI IEGRDSTKGE DGASKKDEAT N
//
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