ID A0A077EEF5_9FLAO Unreviewed; 845 AA.
AC A0A077EEF5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=ClpB protein {ECO:0000313|EMBL:AIL43870.1};
GN ORFNames=BD94_0095 {ECO:0000313|EMBL:AIL43870.1};
OS Elizabethkingia anophelis NUHP1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Elizabethkingia.
OX NCBI_TaxID=1338011 {ECO:0000313|EMBL:AIL43870.1, ECO:0000313|Proteomes:UP000028933};
RN [1] {ECO:0000313|EMBL:AIL43870.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NUHP1 {ECO:0000313|EMBL:AIL43870.1};
RX PubMed=24012265; DOI=10.1016/S0140-6736(13)61858-9;
RA Teo J., Tan S.Y., Tay M., Ding Y., Kjelleberg S., Givskov M., Lin R.T.,
RA Yang L.;
RT "First case of E anophelis outbreak in an intensive-care unit.";
RL Lancet 382:855-856(2013).
RN [2] {ECO:0000313|EMBL:AIL43870.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NUHP1 {ECO:0000313|EMBL:AIL43870.1};
RX PubMed=26019164; DOI=10.1093/gbe/evv101;
RA Li Y., Liu Y., Chew S.C., Tay M., Salido M.M., Teo J., Lauro F.M.,
RA Givskov M., Yang L.;
RT "Complete Genome Sequence and Transcriptomic Analysis of the Novel Pathogen
RT Elizabethkingia anophelis in Response to Oxidative Stress.";
RL Genome Biol. Evol. 7:1676-1685(2015).
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
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DR EMBL; CP007547; AIL43870.1; -; Genomic_DNA.
DR RefSeq; WP_009090303.1; NZ_CP007547.1.
DR AlphaFoldDB; A0A077EEF5; -.
DR STRING; 1338011.BD94_0095; -.
DR GeneID; 56685180; -.
DR KEGG; eao:BD94_0095; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_10; -.
DR Proteomes; UP000028933; Chromosome.
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 Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..71
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 441..476
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 149..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 437..483
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 149..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 845 AA; 95403 MW; 4476729412F6A368 CRC64;
MEYQFSKGMN QVFNNSRNEA KRLQSEFLNT EHLLLGIIKS ENSSAYAILE DFNADLTQIR
RKIESLNITS NNPNAMVTEK IPLTKMADQA IKRAALECRL YKSTEVNTVH LLLGILYKTE
DPTTSILESY DIDYQAVSKH YKSMLKENGD LPKNQAFDDD EDKDDAFSQM KKPSGNLGTG
KSKTPVLDNF GRDLTGLARD GKLDPVIGRE KEIERVSQIL SRRKKNNPLL IGEPGVGKSA
IAEGLALRIH QKKVSRVLFN KRVITLDLAS LVAGTKYRGQ FEERMKAIMS ELEKNRDVIL
FIDELHTIVG AGSSTGSLDA SNMFKPALAR GEIQCIGATT LDEYRQYIEK DGALERRFQK
VMVEPTTIEE SIQILNQIKD KYEEYHNVTY TDDAIKACVN LTARYITDRF LPDKAIDALD
EAGSRVYIKN MKVPTEIIEY EKAIEEVKEQ KQKAVKAQDY LEARKLKDEE ERLQIELNLA
QENWDKEVKE KKEVVTEENV AEVVSMMSGV PVTKVGKNEL DKLSQMDAML NGKVIGQEDA
VRKVVKAIQR NRAGLKDPNR PIGTFIFLGT TGVGKTELAK VMARELFDSD EALIRIDMSE
YMEKFAVSRL VGAPPGYVGY EEGGQLTEAV RRKPYAVVLL DEIEKAHPDV FNILLQILDE
GHVTDSLGRK VDFRNTIIIL TSNIGTRDLK DFGDGVGFGT SAKKSTSDTR ARSTIENALK
KAFAPEFLNR IDDIIIFNSL EKDDIKKIIN LELGKLYSRL EKLDYHVELS EEATEFIAEK
GWDKDFGARP LKRAIQKYIE DLLAEMLVNK QMKEGDKIVL KLNEAKDALE AEKSPKKKEK
EPKTS
//
