ID K2P2W7_9FLAO Unreviewed; 850 AA.
AC K2P2W7;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=ATPase {ECO:0000313|EMBL:EKF55363.1};
GN ORFNames=I215_07851 {ECO:0000313|EMBL:EKF55363.1};
OS Galbibacter marinus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Galbibacter.
OX NCBI_TaxID=555500 {ECO:0000313|EMBL:EKF55363.1, ECO:0000313|Proteomes:UP000007364};
RN [1] {ECO:0000313|EMBL:EKF55363.1, ECO:0000313|Proteomes:UP000007364}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ck-I2-15 {ECO:0000313|Proteomes:UP000007364};
RX PubMed=23209227; DOI=10.1128/JB.01852-12;
RA Lai Q., Li C., Shao Z.;
RT "Genome Sequence of Galbibacter marinum Type Strain ck-I2-15.";
RL J. Bacteriol. 194:6973-6973(2012).
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKF55363.1}.
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DR EMBL; AMSG01000008; EKF55363.1; -; Genomic_DNA.
DR RefSeq; WP_008991425.1; NZ_AMSG01000008.1.
DR AlphaFoldDB; K2P2W7; -.
DR STRING; 555500.I215_07851; -.
DR PATRIC; fig|555500.3.peg.1627; -.
DR eggNOG; COG0542; Bacteria.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000007364; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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 Gene3D; 4.10.860.10; UVR domain; 1.
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; 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 InterPro; IPR001943; UVR_dom.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF193; CHAPERONE PROTEIN CLPB; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 2.
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.
DR PROSITE; PS50151; UVR; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000007364};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..150
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 449..484
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 151..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 445..491
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 161..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 850 AA; 95306 MW; 49849DECBBEED18B CRC64;
MDDNFSPRVK DVIAYSKEEA LRLGHDFIGT EHLMLGLLRD GNGKAIDILS ALSVDLDHLR
RKVEILSPSN LSVGVSANDK RNLHLTRQAE RALKTTFLEA KLFQSPSINT AHLLLCILRN
ENDPTTKLLN KLKIDYDNAK EQFKLMITSE DDFLDPPTAD SFSDETGSAE EGNNPFGSSA
SNNPKTNKKS KTPVLDNFGR DLTLLAEEEK LDPVVGREKE IERVSQILSR RKKNNPLLIG
EPGVGKSAIA EGLALRIVKK KVSRILYNKR VVTLDLASLV AGTKYRGQFE ERMKAVMNEL
EKNDDIILFI DEIHTIVGAG GATGSLDASN MFKPALARGE IQCIGATTLD EYRQYIEKDG
ALERRFQKVI VEPTSVVETI EILHNIKDKY EEHHNVNFTD QAIEACVKLT NRYLTDRFLP
DKAIDALDEA GSRVHIINME VPKQILDLEK ELDRVKELKN SVVKKQKYEE AAKLRDDEKR
IERELSQAQE KWEEDSKLHR EIVTDENVAD VVSMMSGVPV TRIAQAESSK LAQMPDLIKG
KVIGQDNAVA KVVKAIQRNR AGLKDPDKPI GSFIFLGQTG VGKTQLAKVL AKQLFDSEDA
LVRIDMSEYM EKFAVSRLIG APPGYVGYEE GGQLTEKIRR KPYAVILLDE VEKAHPDVFN
MLLQVLDDGY ITDSLGRKID FRNTIIIMTS NIGARQLKDF GQGVGFGTSA KQAQADEHSK
SVIENALKKA FAPEFLNRID DVVVFNPLEK EDIHKIIDIE LEKLYQRIEG LGYYLSLSEQ
AKDYIADKGF DRQYGARPLK RAIQKYIEDA LAEEIIASKI AEGDRIEMDL SEEKDALTIK
ISKVEKSTES
//
