ID A0A2I1JB81_9MICC Unreviewed; 871 AA.
AC A0A2I1JB81;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=NDP-hexose 4-ketoreductase {ECO:0000313|EMBL:PKY80623.1};
GN ORFNames=CJ193_06545 {ECO:0000313|EMBL:PMC77772.1}, CYJ35_02370
GN {ECO:0000313|EMBL:PKY80623.1};
OS Pseudoglutamicibacter albus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Pseudoglutamicibacter.
OX NCBI_TaxID=98671 {ECO:0000313|EMBL:PKY80623.1, ECO:0000313|Proteomes:UP000234591};
RN [1] {ECO:0000313|EMBL:PMC77772.1, ECO:0000313|Proteomes:UP000235423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMB0715 {ECO:0000313|EMBL:PMC77772.1,
RC ECO:0000313|Proteomes:UP000235423};
RA Thomas-White K., Kumar N., Forster S., Putonti C., Lawley T., Wolfe A.J.;
RT "Bacterial strain isolated from the female urinary microbiota.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PKY80623.1, ECO:0000313|Proteomes:UP000234591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMB0722 {ECO:0000313|EMBL:PKY80623.1,
RC ECO:0000313|Proteomes:UP000234591};
RA Thomas-White K., Wolfe A.J.;
RT "Phylogenetic diversity of female urinary microbiome.";
RL Submitted (DEC-2017) 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:PKY80623.1}.
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DR EMBL; PKGR01000002; PKY80623.1; -; Genomic_DNA.
DR EMBL; PNHO01000018; PMC77772.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I1JB81; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000234591; Unassembled WGS sequence.
DR Proteomes; UP000235423; 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; -; 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:SF155; CLP PROTEASE ATP-BINDING SUBUNIT; 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 Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
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 426..461
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 148..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 816..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 422..468
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 838..855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 871 AA; 95756 MW; 86EFBE35736EFE76 CRC64;
MFERFTDRAR RVVVLAQEEA RMLNHTYIGT EHILLGLIHE GEGVAAKSLE SLNVTLGAVR
EQVQEIIGQG SQAPTGHIPF TPRAKKVLEL SLREALQLGH NYIGTEHILL GLIREGEGTA
AQVLNSLGAD PQAVRQEVIQ LISGYHSSKE PAGAGGGSRD QKEGTPSGSA VLDQFGRNLT
AAARENKLDP VIGREHEMER VMQVLSRRTK NNPVLIGEPG VGKTAVVEGL AQAIVRGDVP
ETLKDKHLYT LDLGSLVAGS RYRGDFEERL KKVLKEIRTR GDIILFIDEI HTLVGAGAAE
GAIDAASILK PMLARGELQT IGATTLDEYR KHIEKDAALE RRFQPIQVPE PSVELTVEIL
RGLRDKYEAH HRVSITDEAL QSAAQLAHRY ISDRFLPDKA VDLIDEAGAR LRIQRMTAPP
ELKEMDQKIA DIRREKESAI DAQDFEGAAK LRDEEQRLIT ERQEKEAAWK NGDLDEISEV
TPEVIAEVLA SSTGIPVVQL TEEESTRLLN MEDELHKRII GQDEAIKSIA RSIRRTRAGL
KDPNRPGGSF IFAGPTGVGK TELAKALAEF MFGDEDALIT LDMSEYAEKH TVSRLFGAPP
GYVGYEEGGQ LTEKVRRRPF SIVLFDEVEK AHADLFNSLL QILEDGRLTD SQGRVVDFKN
TIIIMTTNLG TRDISKGVMT GFQSTTDVQT GYERMQAKVQ EELRQHFRPE FLNRVDDIVV
FPQLQHSEIV QIVDLFTDRL SERLGERSIS LKVTQPARDL LADRGFDPAM GARPLRRTIQ
RDVEDPLSEK ILFGELLPGQ TVVVDVEGEE GSRKLTFTAV DGPDQLEGKA SPAAILAGST
EPTGTSESES GTGEAGTDEA GTGEASADDR A
//