ID U5D658_9CHRO Unreviewed; 797 AA.
AC U5D658;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=ATPase with chaperone activity, ATP-binding subunit {ECO:0000313|EMBL:ERN40113.1};
GN ORFNames=KR51_00034000 {ECO:0000313|EMBL:ERN40113.1};
OS Rubidibacter lacunae KORDI 51-2.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Rubidibacter.
OX NCBI_TaxID=582515 {ECO:0000313|EMBL:ERN40113.1, ECO:0000313|Proteomes:UP000016960};
RN [1] {ECO:0000313|EMBL:ERN40113.1, ECO:0000313|Proteomes:UP000016960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KORDI 51-2 {ECO:0000313|EMBL:ERN40113.1,
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 -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, 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:ERN40113.1}.
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DR EMBL; ASSJ01000081; ERN40113.1; -; Genomic_DNA.
DR RefSeq; WP_022609007.1; NZ_ASSJ01000081.1.
DR AlphaFoldDB; U5D658; -.
DR STRING; 582515.KR51_00034000; -.
DR PATRIC; fig|582515.4.peg.3816; -.
DR eggNOG; COG0542; Bacteria.
DR InParanoid; U5D658; -.
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; -; 1.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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 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.
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|ARBA:ARBA00023054};
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}.
FT DOMAIN 2..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 151..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 797 AA; 87769 MW; 9165DB248DEDA00B CRC64;
MFEHFTDKAI KSVMLAQEEA RRMRQNLVGS EQILLGLVGE GTSTAARLLA EQSVTLKVGR
QAVEESIGRG SFGSSANIPF TPKAKRVFEQ ALQIARQHEH KHISPEHLLY ALITEESVAV
KVLGKLSVDL EQLQENLQAF FETDSSVKSE AATVGGRPTR SAFGSNSRSP RGSLAEFGTD
LTQKAAEDRL DPIIGRDKEV ERAIQILGRR TKNNPILVGE PGVGKTAIAE GLAQRIVRND
VPEALRDRRV IGLDMAALVA GTRFRGEFEE RLKAIVSEVR EAGNIILVID EIHTLIGGGV
MDGGLDAANL LKPALARGEL QCLGTTTLDE YRKYIEQDAA LERRFQRILI DEPTVDETIE
ILQGLRAPYE EFHKVRIAES AMEAAAKLSD RYIADRFLPD KAIDLIDEAG SRLHLRQSME
RKQATIGGEP SGDRLDDNTS CEYPVVSSED IAQIVASWTG VPVSKLTETE SELLLHLEES
LHQRVIGQDE AVTAVARAVR RARAGIKDPN RPIASFIFCG PTGVGKTELS KALAAYMFGD
EAAMVRLDMS EYMDRYSVSK LIGSPPGFVG YDEGGQLTEA VRRRPYTVVL FDEIEKAHPD
IFNLLLQVLD DGHLTDAHGR SVDFNNTVLI LTSNLGSKAI EKGGGGLGFE LATDADSARY
QRIRDRVNEE LKNTFRPEFI NRLDEVVVFR QLLRDELARI ADLILEDIRT RLHEQQDIGL
EVTAAFKARA IEVGFDPAYG ARPLRRALTH MLEDRLAEAI LADALRAGNI AVADIAADGD
ILIAAREQKE LVLQASR
//