ID A0A1H7M5D4_9GAMM Unreviewed; 761 AA.
AC A0A1H7M5D4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:SEL06466.1};
GN ORFNames=SAMN05428989_1347 {ECO:0000313|EMBL:SEL06466.1};
OS Pseudoxanthomonas sp. GM95.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=1881043 {ECO:0000313|EMBL:SEL06466.1, ECO:0000313|Proteomes:UP000199164};
RN [1] {ECO:0000313|Proteomes:UP000199164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM95 {ECO:0000313|Proteomes:UP000199164};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675}.
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DR EMBL; FOAX01000001; SEL06466.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7M5D4; -.
DR STRING; 1881043.SAMN05428989_1347; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000199164; 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: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; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:SEL06466.1};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Hydrolase {ECO:0000313|EMBL:SEL06466.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:SEL06466.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 144..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 761 AA; 83297 MW; 3A3487D11DC6E2F4 CRC64;
MFSKDLEQTI GQCYKRAREA RHEFMTVEHL LLALLDNPSA QAVLKATGAD TGRLRTDLDQ
AVEASVSRLA EDDGRDTQPT LGFQRVLQRA VYHVQSSGKK EVTGANVLVA IFGEKDSHAV
YFLNQQDVTR LDIVNYLSHG IAKQGEGEPQ ASSGDAAEGK AEGGEGEAKG DALAEYASNL
NEAARNGKID PLVGRAEEIE RTIQVLCRRR KNNPLYVGEA GVGKTALAEG LAKRIVDGEV
PEVLEDAVIY SLDLGALVAG TKYRGDFEKR LKAVLGALKK VPNAVLFIDE IHTIIGAGSA
SGGTMDASNL IKPALASGEL RCIGSTTFQE YRGIFEKDRA LARRFQKIDV VEPTIAETYE
ILQGLKPKYE SHHNVSYADD ALQAAVDLSV KHIGDRLLPD KAIDVIDEAG ARQRLLPEEQ
RKTLIDIEEI ETIVAKMARI PAKQVSATDK DVLQHLERNL KMVIFGQDPA IESLASAIKL
ARSGLGNPEK PIGNFLFAGP TGVGKTEVTK QLAMQLGIEL VRFDMSEYME PHSISRLIGA
PPGYVGFDQG GLLTEKIVKT PHCVLLLDEV EKAHPDIFNI LLQVMDRGVL TDTNGREANF
KNVILVMTTN AGAAQASRRS IGFTKQDHST DAMEVIRRGF TPEFRNRLDA IVQFQALGFD
HILRVVDKFL IELEMLLHEK HVTLSATPEA RDWLAQHGFD PQMGARPMAR VIQDKIKRPL
ADELLFGKLI GGGRVSIDVK DDELVVTAQS EPERLLPATV D
//