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Database: UniProt
Entry: A0A1V2Q0T3_9PSEU
LinkDB: A0A1V2Q0T3_9PSEU
Original site: A0A1V2Q0T3_9PSEU 
ID   A0A1V2Q0T3_9PSEU        Unreviewed;       852 AA.
AC   A0A1V2Q0T3;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=NDP-hexose 4-ketoreductase {ECO:0000313|EMBL:ONI81824.1};
GN   ORFNames=ALI22I_37100 {ECO:0000313|EMBL:ONI81824.1};
OS   Saccharothrix sp. ALI-22-I.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharothrix.
OX   NCBI_TaxID=1933778 {ECO:0000313|EMBL:ONI81824.1, ECO:0000313|Proteomes:UP000188617};
RN   [1] {ECO:0000313|EMBL:ONI81824.1, ECO:0000313|Proteomes:UP000188617}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ALI-22-I {ECO:0000313|EMBL:ONI81824.1,
RC   ECO:0000313|Proteomes:UP000188617};
RX   PubMed=28087533;
RA   Yeager C.M., Gallegos-Graves V., Dunbar J., Hesse C.N., Daligault H.,
RA   Kuske C.R.;
RT   "Polysaccharide degradation capability of Actinomycetales soil isolates
RT   from a semi-arid grassland of the Colorado Plateau.";
RL   Appl. Environ. Microbiol. 0:0-0(2017).
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:ONI81824.1}.
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DR   EMBL; MTQP01000068; ONI81824.1; -; Genomic_DNA.
DR   RefSeq; WP_077010286.1; NZ_MTQP01000068.1.
DR   AlphaFoldDB; A0A1V2Q0T3; -.
DR   STRING; 1933778.ALI22I_37100; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000188617; Unassembled WGS sequence.
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; 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; PS00870; CLPAB_1; 1.
DR   PROSITE; PS50151; UVR; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000188617};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          2..144
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          422..457
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          821..852
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   852 AA;  94559 MW;  AC964A2802D9669B CRC64;
     MFERFTDRAR RVVVLAQEEA RMLNHNYIGT EHILLGLIHE GEGVAAKALE SLGIALEGVR
     QQVEEIIGQG QQAPSGHIPF TPRAKKVLEL SLREALQLGH NYIGTEHILL GLIREGEGVA
     AQVLVKLGAD LNRVRQQVLQ LLSGYSGGKE PAESGGRGEG TPSSSLVLDQ FGRNLTASAR
     EGKLDPVIGR TKEIERVMQV LSRRTKNNPV LIGEPGVGKT AVVEGLAQMV VKGEVPETLK
     DKQLYTLDLG SLVAGSRYRG DFEERLKKVL KEIRTRGDII LFIDEIHTLV GAGAAEGAID
     AASILKPMLA RGELQTIGAT TLDEYRKYVE KDPALERRFQ PIQVGEPSLE HTIEILKGLR
     DRYEAHHRVS ITDSALVAAA TLADRYINDR FLPDKAIDLI DEAGARMRIR RMTAPPDLRE
     FDEKIADVRR DKESAIDAQD FERAAKLRDA EKQLLGQKAE REKQWKDGDL DVVAEVDDEQ
     IAEVLANWTG IPVFKLTEEE TSRLLRMEDE LHKRIIGQVD AVRAVSQAIR RTRAGLKDPK
     RPSGSFIFAG PSGVGKTELS KALANFLFGE DDALIQIDMG EFHDRYTASR LFGAPPGYVG
     YEEGGQLTEK VRRKPFSVVL FDEIEKAHQE VYNTLLQVLE DGRLTDGQGR TVDFKNTVII
     FTSNLGTSDI SKAVGLGFTS GQDTASNYER MKNKVNDELK KHFRPEFLNR IDDIIVFHQL
     TQDEIIKMVD LMIARVETQL KNKDMAIELT DRAKMLLAKR GFDPVLGARP LRRTIQREIE
     DQLSEKILFG EIQPGHIIIT DVEGWDGESE ADDKAHFVFR GEPKPLRVPD APPVDLASSG
     GDSGGESDSE SA
//
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