ID F6GJK4_LACS5 Unreviewed; 852 AA.
AC F6GJK4;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=ATPase AAA-2 domain protein {ECO:0000313|EMBL:AEH02449.1};
GN OrderedLocusNames=Lacal_2608 {ECO:0000313|EMBL:AEH02449.1};
OS Lacinutrix sp. (strain 5H-3-7-4).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Lacinutrix.
OX NCBI_TaxID=983544 {ECO:0000313|EMBL:AEH02449.1, ECO:0000313|Proteomes:UP000008297};
RN [1] {ECO:0000313|EMBL:AEH02449.1, ECO:0000313|Proteomes:UP000008297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5H-3-7-4 {ECO:0000313|EMBL:AEH02449.1,
RC ECO:0000313|Proteomes:UP000008297};
RX PubMed=21725025; DOI=10.1128/JB.05518-11;
RA Klippel B., Lochner A., Bruce D.C., Walston Davenport K., Detter C.,
RA Goodwin L.A., Han J., Han S., Hauser L., Land M.L., Nolan M.,
RA Ovchinnikova G., Pennacchio L., Pitluck S., Tapia R., Woyke T.,
RA Wiebusch S., Basner A., Abe F., Horikoshi K., Keller M., Antranikian G.;
RT "Complete genome sequences of Krokinobacter sp. strain 4H-3-7-5 and
RT Lacinutrix sp. strain 5H-3-7-4, polysaccharide-degrading members of the
RT family Flavobacteriaceae.";
RL J. Bacteriol. 193:4545-4546(2011).
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
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DR EMBL; CP002825; AEH02449.1; -; Genomic_DNA.
DR RefSeq; WP_013871228.1; NC_015638.1.
DR AlphaFoldDB; F6GJK4; -.
DR STRING; 983544.Lacal_2608; -.
DR KEGG; lan:Lacal_2608; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_10; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000008297; 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 Reference proteome {ECO:0000313|Proteomes:UP000008297};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..149
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 451..486
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 149..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 447..493
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 168..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 852 AA; 95324 MW; C8BBA53F5AAB08E1 CRC64;
MDDNFSPRVK DVIAYSKEEA LRLGHDFIGT EHLMLGLLRD GNGKAINILN ALDIDLNHLR
RKVEILSPAN PNVTITSNEK KNLHLTRQAE RALKTTFLEA KLFQSTSINT AHLLLCILRN
ENDPTTKLLN KLKVDYDNVK EQFKSMITSD DNFTDNSGEP KAESFQDDAQ GSDGNESKDI
FNTPSGKGNK KSKTPVLDNF GRDLTAMAEE GKLDPVVGRE KEIERVSQIL SRRKKNNPLL
IGEPGVGKSA IAEGLANRIV KRKVSRILFN KRVVTLDLAS LVAGTKYRGQ FEERMKAVMN
ELEKNDDVIL FIDEIHTIVG AGGATGSLDA SNMFKPALAR GEIQCIGATT LDEYRQYIEK
DGALERRFQK VIVEPTTVEE TIEILNNIKG KYEEHHNVDY TDAAIEACVK LTNRYMTERF
LPDKAIDALD EAGSRVHITN IDVPKQIIEL EKKLEEVKAT KNSVVKKQKY EEAARLRDDE
KRIEKELAIA QEKWEEDTKL HKVTVTEDNV ADVISMMTGV PVNRIAQTES NKLAELPELI
KGKVIGQDDA VAKVVKAIQR NRAGLKDPNK PIGSFIFLGQ TGVGKTQLAK VLSRELFDSE
ESLIRIDMSE YMEKFAISRL VGAPPGYVGY EEGGQLTEKV RRKPYAVVLL DEIEKAHPDV
FNMLLQVLDD GYLTDSLGRK IDFRNTIIIM TSNIGARKLK DFGTGIGFGT ASQKSQEDAN
ARAVIQNALK KSFAPEFLNR IDDVVVFNAL EKEDINKIID IELDKLLIRI KGLGYTLQLT
DTAKNYIADK GFDKQYGARP LKRAIQKYVE DALAEEIITS SITDGDIIKM DLDDKTDEIK
ITIEKAQKST ES
//
