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}.
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; 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
//