ID K9EVW6_9ACTO Unreviewed; 866 AA.
AC K9EVW6;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Clp R domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF9233_00893 {ECO:0000313|EMBL:EKU95132.1};
OS Actinobaculum massiliense ACS-171-V-Col2.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinobaculum.
OX NCBI_TaxID=883066 {ECO:0000313|EMBL:EKU95132.1, ECO:0000313|Proteomes:UP000009888};
RN [1] {ECO:0000313|EMBL:EKU95132.1, ECO:0000313|Proteomes:UP000009888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-171-V-Col2 {ECO:0000313|Proteomes:UP000009888};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Saerens B., Vaneechoutte M.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Actinobaculum massiliae ACS-171-V-COL2.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:EKU95132.1}.
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DR EMBL; AGWL01000005; EKU95132.1; -; Genomic_DNA.
DR RefSeq; WP_007001099.1; NZ_JH992955.1.
DR AlphaFoldDB; K9EVW6; -.
DR STRING; 202789.GCA_001457435_01228; -.
DR PATRIC; fig|883066.3.peg.932; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_11; -.
DR Proteomes; UP000009888; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000009888};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 2..144
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 422..457
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 813..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..866
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 866 AA; 95574 MW; 1AF2A89A9DFE2587 CRC64;
MFERFTDRAR RVIVLAQEEA RNLKHNYLGT EHVLLGLIRE GEGVAAKALE ALGITLDEVR
AEVIEIIGEG QEQPSGHIPF TPRAKKVIEY AMREGLQLGH SYIGTEHLLL GLTREPDGVA
AQVLQKLGAD MPTVRNQVNQ LISGFQGKEA VGVGGGRREG QKAGSTILDQ YGRNLTQAAR
DHKLDPVIGR HTETERVMQV LSRRTKNNPV LIGEPGVGKT AVVEGLSQMI AADNVPETLK
GKQLYSLDMG SLVAGSRYRG DFEERMKKIL KEINTRGDII LFIDEIHTLV GAGAAEGALD
AASLLKPMLA RGEIQVIGAT TLDEYRKYIE KDAALERRFQ PIQVDQPTAE QTIEILKGLR
DRYESYHRVT ITDDALEAAA TLSERYINDR FLPDKAIDLI DEAGARLAIR KMTAPPELRE
LDEKISSTRR AKEAAIDGQD FERAAKLRDE EQSLNAERDE KEKAWKDGDM DVVSVVDEDL
ITEVLSMSTG IPVFKLSEAE SEKLLRMEDE LHKRVIGQHE AVTAISQAIR RQRAGLKDPN
RPGGSFIFAG PTGVGKTELA KALAEFLFGD ESALITLDMS EYSEKHTVSR LFGAPPGYVG
YEEGGQLTEA VRRKPFSVVL FDEIEKAHAD LFNSLLQILE EGRLTDSQGR VVDFKNTIII
MTTNLGTKDI AKGVQTGFQF DQDTTTSYER MKMKVSEELK SHFRPEFLNR VDDVIVFPQL
GRDEILQIVD LMIGKLDKRL RGQKLSIALT KDAKELLADR GYDPVLGARP LRRAIQRDIE
DVLSEKLLYG EFEDGQVIVV DVDKNDIPMS FTFKGQDASE PLPAGVGEVE APPEMESLVS
KTSSSGRLGS TSGPSAPSSG GLQAAN
//
