ID A0A255EM47_9ACTN Unreviewed; 839 AA.
AC A0A255EM47; A0A255E560;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=NDP-hexose 4-ketoreductase {ECO:0000313|EMBL:OYN92586.1};
GN ORFNames=CGZ91_03670 {ECO:0000313|EMBL:OYN92586.1}, CGZ92_12495
GN {ECO:0000313|EMBL:OYN84645.1};
OS Parenemella sanctibonifatiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Parenemella.
OX NCBI_TaxID=2016505 {ECO:0000313|EMBL:OYN92586.1, ECO:0000313|Proteomes:UP000216300};
RN [1] {ECO:0000313|Proteomes:UP000216300, ECO:0000313|Proteomes:UP000216533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML 150081 {ECO:0000313|EMBL:OYN92586.1,
RC ECO:0000313|Proteomes:UP000216300}, and NML 160184
RC {ECO:0000313|EMBL:OYN84645.1, ECO:0000313|Proteomes:UP000216533};
RA Bernier A.-M., Bernard K., Domingo M.-C.;
RT "Draft whole genome sequences of clinical Proprionibacteriaceae strains.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {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:OYN92586.1}.
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DR EMBL; NMVI01000027; OYN84645.1; -; Genomic_DNA.
DR EMBL; NMVJ01000001; OYN92586.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255EM47; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000216300; Unassembled WGS sequence.
DR Proteomes; UP000216533; 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; IPR028299; ClpA/B_CS2.
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:SF193; CHAPERONE PROTEIN CLPB; 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.
DR PROSITE; PS50151; UVR; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000216300};
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 421..456
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 807..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 839 AA; 92943 MW; 06139A0573D18BD6 CRC64;
MFERFTDRAR RVVVLAQDEA RMLNHNYIGT EHILLGLIHE GEGVAAKALD SLGVTLEDAR
EQVVEMIGHG QQAPTGHIPF TPRAKRVLEL SLREAIQINH SYIGTEHILL GLIREGEGIA
TQVLIKLGAD LARVRSTVLQ MLNGYQGKEA ATAGAPEQGA PSSSSVLDQF GRNLTQAAKD
NALDPVIGRE KEIERVMTVL SRRTKNNPVL IGEPGVGKTA VVEGLSQAVV RGDVPETLRD
KQIYTLDLGA LVAGSRYRGD FEERLKKVLK EIKSRGDIIL FIDEIHTLVG AGAAEGAIDA
ASILKPMLAR GELQTIGATT LDEYRKHIEK DAALERRFQP IQVAEPSIAH TIDILRGLRD
RYEAHHRVTI TDEALTAAAT MADRYVQDRF LPDKAIDLID EAGARLRIKR MTAPPDLREF
DEKIAQVRLE KEAAIDGQDY ERAARLRDDE KKLLNQRSEK EEAWKVGDTD TVAEVDDELI
AEVLSSATGI PVFRITEEES SRLLNMEQEI GKRYIGQDEA VKALARSIRR TRAGLKDPKR
PSGSFIFAGP SGVGKTELTK ALTEFLFGDE DALITLDMSE YSEKHTASRM FGSPPGYVGY
EEGGQLTEKV RRKPFSVVLF DEIEKAHPDI FNSLLQILDE GRLTDAQGRV VDFKNTVIVM
TTNLGTRDIA KTVNLGFSAA NDTEGSYERM KGKVAEELKQ NFRPEFLNRI DEIIVFRQLT
QEDIERIVDL MVAEIEVRLK DRDMGIELTQ PAKELVAKRG FDPVLGARPL RRALQRDIED
VLAEKILFGE LGAGQIVRVD VNEGDKEQPF TFEGTAKSDL PDSPSELELA TDEGGATGE
//
