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
//