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Database: UniProt
Entry: A0A2W1TYY9_9MICO
LinkDB: A0A2W1TYY9_9MICO
Original site: A0A2W1TYY9_9MICO 
ID   A0A2W1TYY9_9MICO        Unreviewed;       722 AA.
AC   A0A2W1TYY9;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=ATP-dependent chaperone ClpB {ECO:0000313|EMBL:PZE86213.1};
GN   ORFNames=DEI91_03655 {ECO:0000313|EMBL:PZE86213.1};
OS   Curtobacterium sp. MCBD17_032.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Curtobacterium.
OX   NCBI_TaxID=2175659 {ECO:0000313|EMBL:PZE86213.1, ECO:0000313|Proteomes:UP000248716};
RN   [1] {ECO:0000313|EMBL:PZE86213.1, ECO:0000313|Proteomes:UP000248716}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCBD17_032 {ECO:0000313|EMBL:PZE86213.1,
RC   ECO:0000313|Proteomes:UP000248716};
RA   Chase A.B., Gomez-Lunar Z., Lopez A.E., Li J., Allison S.D., Martiny A.C.,
RA   Martiny J.B.H.;
RT   "Emergence of Soil Bacterial Ecotypes Along a Climate Gradient.";
RL   Submitted (JUN-2018) 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, 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:PZE86213.1}.
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DR   EMBL; QKTO01000002; PZE86213.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2W1TYY9; -.
DR   Proteomes; UP000248716; 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; 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; 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: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; PF10431; ClpB_D2-small; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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, ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248716};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          55..199
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          453..652
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          620..711
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   COILED          269..349
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   722 AA;  80018 MW;  CB21B5EBDE47895C CRC64;
     MANLQGAPDS QEKQKTALQQ YGVDLTAIAR SGKLDPVIGR DAEIRRVSQV LTRRTKNNPV
     LIGEPGVGKT AVVEGLAQRI VAGDVADSLK DKRLVSLDMS ALIAGAKYRG EFEERLKAVL
     KEIDDSDGQV ITFIDELHTL MGAGGGEGSV AASNMLKPML ARGELRLIGA TTLDEYREYI
     EKDAALERRF QQVYVGEPSV EDTVAILRGL KERYEAHHKV TINDSALVAA SALSDRYIAG
     RQLPDKAIDL IDEAASRLRM EIDSSPVEID ELKRTVDRLR VEEFALKQEK DDASKARLET
     LRDELRSRGE LLDGLEARWQ AERTTLNRIG ELKQQLDDLN MRSQRAQREA DYETVSRLEY
     GEKPRIEAEL AAAEQAGSTD RMVNDSVTDE DIAAVIAQWT GIPVGRLLQG ETEKLLHLER
     ELGRRIIGQR TAVAAVSEAV RRTRAGISDP DRPTGSFLFL GPTGVGKTEL AKALAEFLFD
     DEKALVRIDM SEYGEKHSVA RLIGAPPGYV GYEAGGQLTE AVRRRPYSVI LLDEIEKAHP
     EVFDVLLQVL DDGRLTDGQG RTVDFRNTIL VLTSNLGSQF LTDPALSNEQ REAAVREMVQ
     QAFRPEFLNR LDDMVVFQAL TPDDLAQIVS LYVDRLARRL SGRRLELAVT PDARAWLAER
     GYEPAYGARP LRRLMQRQID DQLARAILAG DVRDGDAVRV DVAPGGEQLT VEPFEVAEIV
     EE
//
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