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Database: UniProt
Entry: A0A5J5IWB0_9MICO
LinkDB: A0A5J5IWB0_9MICO
Original site: A0A5J5IWB0_9MICO 
ID   A0A5J5IWB0_9MICO        Unreviewed;       862 AA.
AC   A0A5J5IWB0;
DT   11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit {ECO:0000313|EMBL:KAA9105603.1};
GN   ORFNames=F6B43_17700 {ECO:0000313|EMBL:KAA9105603.1};
OS   Microbacterium rhizomatis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1631477 {ECO:0000313|EMBL:KAA9105603.1, ECO:0000313|Proteomes:UP000325827};
RN   [1] {ECO:0000313|Proteomes:UP000325827}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 30598 {ECO:0000313|Proteomes:UP000325827};
RA   Tian Z.;
RT   "Mumia zhuanghuii sp. nov. isolated from the intestinal contents of plateau
RT   pika (Ochotona curzoniae) in the Qinghai-Tibet plateau of China.";
RL   Submitted (SEP-2019) 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:KAA9105603.1}.
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DR   EMBL; VYSA01000005; KAA9105603.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5J5IWB0; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000325827; 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   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   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; 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   Hydrolase {ECO:0000313|EMBL:KAA9105603.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:KAA9105603.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000325827};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          38..181
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          172..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..192
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   862 AA;  92497 MW;  46A8DFDF4A8D6532 CRC64;
     MPEDFTPQSD ENGAGAFDEF LARYMAGERA REARSIDLSR FLSSRTQSIL QDAGRFALER
     GQRELDALHV LRVIVQQAPA DDAVRRVGAD PRAIVRAVED RLPAPTDPAG IDGAVIAPSV
     QRALFHAYQV ARASGSTYVD PEHLFFALVI AQDSPAGQVL AQAGVTAEAL TQGARETVTP
     SGETTGETTP DAAASETPML DRFGTDLTAL ATAGDLDPVI GRLDEIEQTI EILSRRTKNN
     PVLVGEAGVG KTAIVEGLAQ AIVAGTVPEQ LRGKRVIALD LPAMLAGTRY RGDFEERLTT
     TMDEVAAHKG ELIVFIDEVH TVVGAGGGGD GAMDAGNILK PRLARGELHL VGATTLKEYR
     VIEKDPALER RFQPVRVGEP SVENAVLILQ GLRGAYEDHH AVTYTDDALR AAVELSDRYL
     SDRVLPDKAI DLIDQAGARL RLRLGVKVDV GALVAELATL EADKNAAVSA EHYEEASRIR
     DAIPDVQARL EAATVSSPSA RSTTDSTGTV DAVVDEAQIA AVISRATGIP VNRLTETERD
     RLALLEDELH ARVVGQDDAV TAVAKAVRRN RTGMGDTHRP VGSFLFLGPT GVGKTELAKA
     LAGSLFDDDT AVIRFDMSEF GERHTVSRLV GAPPGYVGYD EAGQLTERVR RNPYSIVLFD
     EIEKAHPDVF NLLLQVLDDG RLTDGQGRTV DFRNTVIVMT SNLGSEFLAS RSGAIGFIAD
     GGGATGFGSD KDLRDRVMGK LREAMRPEFL NRIDEIVLFR KLAVDQLREI VGLLLGATRA
     RLTKRDVQLD VTAAAIDWIA ENGYEPEYGA RPLRRLIQRE VDDRIADLFV SGELVDGGAA
     TVDAVAGTLV VRAAVAEVAH AA
//
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