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Database: UniProt
Entry: F9YVT4_CAPCC
LinkDB: F9YVT4_CAPCC
Original site: F9YVT4_CAPCC 
ID   F9YVT4_CAPCC            Unreviewed;       847 AA.
AC   F9YVT4;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=Chaperone protein clpB {ECO:0000313|EMBL:AEK23248.1};
DE            EC=3.4.21.53 {ECO:0000313|EMBL:AEK23248.1};
GN   OrderedLocusNames=Ccan_11320 {ECO:0000313|EMBL:AEK23248.1};
OS   Capnocytophaga canimorsus (strain 5).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Capnocytophaga.
OX   NCBI_TaxID=860228 {ECO:0000313|EMBL:AEK23248.1, ECO:0000313|Proteomes:UP000008895};
RN   [1] {ECO:0000313|EMBL:AEK23248.1, ECO:0000313|Proteomes:UP000008895}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5 {ECO:0000313|Proteomes:UP000008895};
RX   PubMed=21914877; DOI=10.1128/JB.05853-11;
RA   Manfredi P., Pagni M., Cornelis G.R.;
RT   "Complete genome sequence of the dog commensal and human pathogen
RT   Capnocytophaga canimorsus strain 5.";
RL   J. Bacteriol. 193:5558-5559(2011).
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; CP002113; AEK23248.1; -; Genomic_DNA.
DR   RefSeq; WP_013997238.1; NC_015846.1.
DR   AlphaFoldDB; F9YVT4; -.
DR   STRING; 860228.Ccan_11320; -.
DR   KEGG; ccm:Ccan_11320; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_1_10; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000008895; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
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   Hydrolase {ECO:0000313|EMBL:AEK23248.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008895};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          2..149
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          446..481
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          161..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   847 AA;  95224 MW;  700B5B178BE3A075 CRC64;
     MSENFSPRVK RIITFSHEEA KRLGSPFIGT EHFVAAILHE GSGKAFEILK ALNIDFILLK
     QRIDTLISVA EGAAFSSPTP ALTMQAQRAI QTTFLETKRS QDSIVNSGHL LLSILRNEND
     PTTKIFKKLN VDYENAKEVL SSHKNLDSDV FNVDMSKDFE DEPQDDFLER PKGENIPPSG
     SNKGGQRKMT VLDNFGRDLT YLAEQGKLDP VIGRDKEIER VSQILSRRKK NNPLLIGEPG
     VGKSAIAEGL ALRIFQKKVS RILYNKRVVS LDLASLVAGT KYRGQFEERM KAIMNELEKN
     DDIILFIDEI HTIVGAGGAA GSLDASNMFK PALARGEIQC IGATTLDEYR QSIEKDGALE
     RRFQKVIVEP TSVEETIEIL HNIKKKYEDH HSVTYTDTAI EACVKLTNRY LTDRFLPDKA
     LDALDEAGSR IHITEMKVPK EILELESQLE NITKEKNLAV SKQQFEEAAR LRDSEKNLEK
     SLGDAHKKWE EYVKEHRDEV TEDHIADVVS MMSGIPVNRI AQTEMNKLAT LGETIKGKII
     GQDAAVEKVI KAIKRNRTGL KDPNKPIGSF IFLGQTGVGK TQLAKVLAKE LFDSEEAMIR
     IDMSEYMEKF STTRLIGAPP GYVGYEEGGQ LTEKVRRKPY SVVLLDEIEK AHPDVFNMLL
     QVLDDGFLTD SLGRKIDFRN CIIIMTSNIG ARQLKDFGQG IGFGTAAKTN QAEAHEKSVI
     ENALKKAFAP EFLNRIDDVI IFNPLDKEDI FRIIDIELNK LYIRIKELGY QIKLSQKARE
     FIAEKGYDRQ YGARPLKRAI QKYVEDLLAE EIVASKIKEG DGIYFDVDSN NESLIINILN
     SKLDSLS
//
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