ID W5IHL2_SCAIO Unreviewed; 882 AA.
AC W5IHL2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Clp R domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF9020_01390 {ECO:0000313|EMBL:EFG26306.1};
OS Scardovia inopinata F0304.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Scardovia.
OX NCBI_TaxID=641146 {ECO:0000313|EMBL:EFG26306.1, ECO:0000313|Proteomes:UP000005777};
RN [1] {ECO:0000313|EMBL:EFG26306.1, ECO:0000313|Proteomes:UP000005777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0304 {ECO:0000313|EMBL:EFG26306.1,
RC ECO:0000313|Proteomes:UP000005777};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Baranova O.V.,
RA Blanton J.M., Tanner A.C., Dewhirst F.E., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.,
RA McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Scardovia inopinata F0304.";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675}.
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:EFG26306.1}.
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DR EMBL; ADCX01000013; EFG26306.1; -; Genomic_DNA.
DR RefSeq; WP_006293780.1; NZ_GG770226.1.
DR AlphaFoldDB; W5IHL2; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_11; -.
DR Proteomes; UP000005777; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 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:SF18; HEAT SHOCK PROTEIN 104; 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; PS00871; CLPAB_2; 1.
DR PROSITE; PS50151; UVR; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000005777};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 2..145
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 426..461
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 817..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 422..468
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 851..882
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 882 AA; 96641 MW; 7C22E6B8BCE81EB7 CRC64;
MFERFTDRAR RVIVLAQEEA RSLKHNYIGT EHLLLGLIRE GEGVAAKALA SKGVELDATR
QQVEEMIGKG SAAPTGHIPF TPHARQVLEL SLREALQLGH SYIGTEHVLL GLIREGEGVG
TQVLVKMGVD VADLRTSVID AIRDTSADAS KNDMTNAGGI TDKSAKSGSS LLDQFGRNLT
EEAREGKLDP VIGRSNEIER VMVILSRRTK NNPVLIGEPG VGKTAVVEGL AQKIVAGDVP
ETLKDKQVYA LDLGSMIAGS RYRGDFEERL KKVFKEIKTR GDIVLFIDEI HTIVGAGSAD
GAMGASDMLK PLLARGELQT IGATTTDEYR KYIEKDAALE RRFQPIQVAE PTIAETIEIL
KGLRKKYEDH HHVTITDAAI QSAAELSARY IQDRNLPDKA IDLIDEAGAR LRIKRLTAPS
ALKELDVKVA KVKADKDKAI ADQDFEKAAS LRDAQEKLEQ ERKDKEKSWR EGESDVSMVV
DEDTIAHVIS SATGIPVFKL TETESKKLLN MEAELHKRVI GQDEAVEALS RSIRRARVGL
KDPKRPSGSF IFAGPTGVGK TELAKALAEY LFDDEDALIR VDMSEFGEKY STSRLFGAPP
GYVGYEEGGE LTEKVRRKPF SVILFDEIEK AHPDIFNTLL QVLDDGHLTD GQGRKVDFKN
TIIIMTTNLG TNKIAQSQST GFNLGGNTET SYQRMKDQVQ SELKEQFRPE FLNRLDDIIV
FKQLTESQVR QIVELDVKAL NDRLFERHMS MELTDAAKDL LAEKGFDPLL GARPLRRVIQ
RDIEDAISEE ILMGKIRENE QIVVNAEGEG ILGEFTFSSH PYEVGGPDGD GTDGDSAQAA
EPLPVGAEVN SAPASSDSSF DSSDSAEATG QAASSESGPV SE
//