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Database: UniProt
Entry: A0A255R9C8_9BACT
LinkDB: A0A255R9C8_9BACT
Original site: A0A255R9C8_9BACT 
ID   A0A255R9C8_9BACT        Unreviewed;       881 AA.
AC   A0A255R9C8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=NDP-hexose 4-ketoreductase {ECO:0000313|EMBL:OYP37272.1};
GN   ORFNames=CGZ80_05750 {ECO:0000313|EMBL:OYP37272.1};
OS   Rhodopirellula sp. MGV.
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=2023130 {ECO:0000313|EMBL:OYP37272.1, ECO:0000313|Proteomes:UP000236615};
RN   [1] {ECO:0000313|EMBL:OYP37272.1, ECO:0000313|Proteomes:UP000236615}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGV {ECO:0000313|EMBL:OYP37272.1,
RC   ECO:0000313|Proteomes:UP000236615};
RA   Araujo J.E., Pylro V.S., Leite L.R., Silva M.C.P., Lemos L.N.,
RA   Lourenco M.V.M., Andreote F.D.;
RT   "Draft Genome Sequence of Rhodopirellula MGV strain isolated from soil of a
RT   Brazilian mangrove.";
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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:OYP37272.1}.
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DR   EMBL; NPDI01000016; OYP37272.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A255R9C8; -.
DR   Proteomes; UP000236615; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000236615};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          2..145
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          433..468
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          151..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          850..881
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          429..475
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        161..176
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   881 AA;  98459 MW;  6EB4A9E43AC93628 CRC64;
     MYERFTDRAR KVMQLANQEA QRFNHEYIGT EHILLGLVKE GSGVAANVLK NLDVDLRKIR
     LEVEKLVQSG PEMVTVGKLP QTPRAKKVIE YSMEEARNLN HSYVGTEHIL LGLLREQEGV
     AAQVLMNLGL KLEDVREEVL NLLGHGLEGA EVGERGGRSS EEGGSSASTK SGKSKTPALD
     SFGRDLTELA RKGELDPVIG RSREIERAIQ ILCRRTKNNP VLLGEAGVGK TAIVEGFAQK
     VIEGEVPEIL ADKRIVVLDL AMMVAGTKYR GQFEERIKAV MTEVRRVKNT ILFIDELHTL
     VGAGGAEGAI DAANVLKPAL ARGEIQCIGA TTLDEYRKYI EKDNALARRF QEIIVEPTAK
     EETIEILKGL RERYEEHHRV QITDDAVVSA VEMSERYITA RCLPDKAIDV IDEAGARVRL
     RTMTRPPDLK EIDEEVEKLN KEKEDAVANQ DFEKAANLRD QAEKLRKKKD QITQDWREKS
     QQTDGVVDEE VIAEVVSKMT GIPLTRLSTE DSLRLMKMEE ELHKRVVSQD LAVSAVAKAV
     RRSRSGLKDP RRPTGSFIFA GPTGVGKTLL AKALAEYMFG DSDALVHIDM SEYMEKHNVS
     RLIGAPPGFV GYEEGGQLTE KIRRRPYAVV LFDEIEKAHP DVFNMLLQVM EEGRLTDSFG
     RNVDFRNTIL IMTTNAGAEA IKNEGGFGFQ KADSDASYES MKKRVMEQIE RVFRPEFLNR
     LDDTIIFRHL TRNDLKMVID FELSKVRERL LDRGLALELE DAAKEFLMRQ GTNLDYGARP
     LRRAIEQRVE DPLSEELLRG TFEGKDTIVV KGILENSDGN AVKHEDVTIT DDGKMIDPDG
     KRVKAVRLEF HGDSRGNVGP KEETVSAGVS EGDKPEGESQ G
//
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