ID U5DMM7_9CHRO Unreviewed; 826 AA.
AC U5DMM7;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=ATPase with chaperone activity, ATP-binding subunit {ECO:0000313|EMBL:ERN42931.1};
GN ORFNames=KR51_00002350 {ECO:0000313|EMBL:ERN42931.1};
OS Rubidibacter lacunae KORDI 51-2.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Rubidibacter.
OX NCBI_TaxID=582515 {ECO:0000313|EMBL:ERN42931.1, ECO:0000313|Proteomes:UP000016960};
RN [1] {ECO:0000313|EMBL:ERN42931.1, ECO:0000313|Proteomes:UP000016960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KORDI 51-2 {ECO:0000313|EMBL:ERN42931.1,
RC ECO:0000313|Proteomes:UP000016960};
RA Choi D.H., Noh J.H., Kwon K.-K., Lee J.-H., Ryu J.-Y.;
RT "Draft genome sequence of Rubidibacter lacunae KORDI 51-2.";
RL Submitted (MAY-2013) 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:ERN42931.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ASSJ01000004; ERN42931.1; -; Genomic_DNA.
DR RefSeq; WP_022603946.1; NZ_ASSJ01000004.1.
DR AlphaFoldDB; U5DMM7; -.
DR STRING; 582515.KR51_00002350; -.
DR PATRIC; fig|582515.4.peg.260; -.
DR eggNOG; COG0542; Bacteria.
DR InParanoid; U5DMM7; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000016960; 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; 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:SF155; CLP PROTEASE ATP-BINDING SUBUNIT; 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:UP000016960};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|ARBA:ARBA00023016}.
FT DOMAIN 2..144
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 416..451
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 149..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 826 AA; 91708 MW; C7CA9D5D952AFE94 CRC64;
MFERFTEKAI KVIMLAQEEA RRLGHNFVGT EQILLGLIGE GTGVAAKVLK SMGVNLKDAR
IEVEKIIGRG SGFVAVEIPF TPRAKRVLEL SLEEARQLGH NYIGTEHLLL GLIREGEGVA
ARVLENLGVD LSKVRTQVIR MLGETAEVST SENRGRTKTP TLDEFGSNLT HMAGEGKLDP
VVGRQKEIER VIQILGRRTK NNPVLIGEPG VGKTAIAEGL AQRIANGDVP DILEEKRVVT
LDIGLLVAGT KYRGEFEERL KKIMDEIRQA GNVVLVIDEV HTLIGAGAAE GAIDAANILK
PALARGELQC IGATTLDEYR KHIERDAALE RRFQPVMVGE PSVEETIEIL RGLRDRYEQH
HKLEITDDAL DAAAKLSDRY ISDRYLPDKA IDLIDEAGSR VRLINSQLPP AAKDLDKELR
QLLKQKDDAV RSQDFDRAGE LRDREMEIKA EIRAIAASRK SDSTEGDSDG PRVDSEEIAH
IVSSWTGVPV SKITQTESAK LLHMEDTLHQ RIIGQEDAVK AVSRAIRRAR VGLKNPNRPI
ASFVFSGPTG VGKTELTKAL AAYFFGAEDA MIRLDMSEFM ERHTVSKLIG SPPGYVGYNE
GGQLTEAVRR RPYTVVLFDE IEKAHPDVFN MLLQILEDGR LTDAKGRTVD FKNTLLIMTS
NIGSKVIEKG GGGLGFELET DSSESQYNRI RSLVNEELKQ YFRPEFLNRI DEIIVFRQLT
RDEVKEIADI LLQEVFSRLT EQDIALQVTE KFKERLVEEG YSPAYGARPL RRAIMRLLED
VMAEEILSGR LREGDTATVD IDDEEGAVKV LTGEPAQQKL LSQAAE
//
