ID Z9JX63_9MICO Unreviewed; 726 AA.
AC Z9JX63;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00195, ECO:0000256|HAMAP-Rule:MF_00238};
DE Includes:
DE RecName: Full=Cytidylate kinase {ECO:0000256|HAMAP-Rule:MF_00238};
DE Short=CK {ECO:0000256|HAMAP-Rule:MF_00238};
DE EC=2.7.4.25 {ECO:0000256|HAMAP-Rule:MF_00238};
DE AltName: Full=Cytidine monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_00238};
DE Short=CMP kinase {ECO:0000256|HAMAP-Rule:MF_00238};
DE Includes:
DE RecName: Full=GTPase Der {ECO:0000256|HAMAP-Rule:MF_00195};
DE AltName: Full=GTP-binding protein EngA {ECO:0000256|HAMAP-Rule:MF_00195};
GN Name=der {ECO:0000256|HAMAP-Rule:MF_00195};
GN Synonyms=cmk {ECO:0000256|HAMAP-Rule:MF_00238};
GN ORFNames=BF93_07145 {ECO:0000313|EMBL:EWS82789.1};
OS Brachybacterium phenoliresistens.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC Brachybacterium.
OX NCBI_TaxID=396014 {ECO:0000313|EMBL:EWS82789.1, ECO:0000313|Proteomes:UP000023067};
RN [1] {ECO:0000313|EMBL:EWS82789.1, ECO:0000313|Proteomes:UP000023067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W13A50 {ECO:0000313|EMBL:EWS82789.1,
RC ECO:0000313|Proteomes:UP000023067};
RA Wang X.;
RT "Genome sequence of Brachybacterium phenoliresistens strain W13A50.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: GTPase that plays an essential role in the late steps of
CC ribosome biogenesis. {ECO:0000256|HAMAP-Rule:MF_00195}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:456216; EC=2.7.4.25;
CC Evidence={ECO:0000256|ARBA:ARBA00001097, ECO:0000256|HAMAP-
CC Rule:MF_00238};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593,
CC ChEBI:CHEBI:456216; EC=2.7.4.25;
CC Evidence={ECO:0000256|ARBA:ARBA00001115, ECO:0000256|HAMAP-
CC Rule:MF_00238};
CC -!- SUBUNIT: Associates with the 50S ribosomal subunit. {ECO:0000256|HAMAP-
CC Rule:MF_00195}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00238}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. EngA (Der) GTPase family.
CC {ECO:0000256|ARBA:ARBA00008279, ECO:0000256|HAMAP-Rule:MF_00195,
CC ECO:0000256|PROSITE-ProRule:PRU01049}.
CC -!- SIMILARITY: Belongs to the cytidylate kinase family. Type 1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009427, ECO:0000256|HAMAP-Rule:MF_00238}.
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:EWS82789.1}.
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DR EMBL; JDYK01000002; EWS82789.1; -; Genomic_DNA.
DR AlphaFoldDB; Z9JX63; -.
DR STRING; 396014.BF93_07145; -.
DR PATRIC; fig|396014.3.peg.419; -.
DR eggNOG; COG0283; Bacteria.
DR eggNOG; COG1160; Bacteria.
DR HOGENOM; CLU_016077_4_0_11; -.
DR Proteomes; UP000023067; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0036430; F:CMP kinase activity; IEA:RHEA.
DR GO; GO:0036431; F:dCMP kinase activity; IEA:RHEA.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006220; P:pyrimidine nucleotide metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR CDD; cd02020; CMPK; 1.
DR CDD; cd01894; EngA1; 1.
DR CDD; cd01895; EngA2; 1.
DR Gene3D; 3.30.300.20; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR HAMAP; MF_00238; Cytidyl_kinase_type1; 1.
DR HAMAP; MF_00195; GTPase_Der; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003136; Cytidylate_kin.
DR InterPro; IPR011994; Cytidylate_kinase_dom.
DR InterPro; IPR031166; G_ENGA.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR016484; GTPase_Der.
DR InterPro; IPR032859; KH_dom-like.
DR InterPro; IPR015946; KH_dom-like_a/b.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR NCBIfam; TIGR00017; cmk; 1.
DR NCBIfam; TIGR03594; GTPase_EngA; 1.
DR NCBIfam; TIGR00231; small_GTP; 2.
DR PANTHER; PTHR43834; GTPASE DER; 1.
DR PANTHER; PTHR43834:SF6; GTPASE DER; 1.
DR Pfam; PF02224; Cytidylate_kin; 1.
DR Pfam; PF14714; KH_dom-like; 1.
DR Pfam; PF01926; MMR_HSR1; 2.
DR PRINTS; PR00326; GTP1OBG.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR PROSITE; PS51712; G_ENGA; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00238};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00238};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00195};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00238, ECO:0000313|EMBL:EWS82789.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00195}; Reference proteome {ECO:0000313|Proteomes:UP000023067};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517, ECO:0000256|HAMAP-
KW Rule:MF_00195};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00238, ECO:0000313|EMBL:EWS82789.1}.
FT DOMAIN 293..456
FT /note="EngA-type G"
FT /evidence="ECO:0000259|PROSITE:PS51712"
FT DOMAIN 466..639
FT /note="EngA-type G"
FT /evidence="ECO:0000259|PROSITE:PS51712"
FT BINDING 7..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00238"
FT BINDING 299..306
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT BINDING 346..350
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT BINDING 408..411
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT BINDING 472..479
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT BINDING 519..523
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT BINDING 584..587
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
SQ SEQUENCE 726 AA; 78874 MW; 85FD519136EF37CE CRC64;
MVVAIDGPAG SGKSTIARRT ALATGGGLLD TGAMYRAVTW TALEDGVDLA DHAAVAALAE
ELDLDLGTDP EDPHVRVRGR DITAEIRTER ISAAVSDVAT NTRLRPVLQR LQREILQSAA
AQRGVCVAEG RDITTVVAPD AEVRVLLSAS EEARMRRRAE ELGLEDSAET RERMHDQVVR
RDRDDSSVSE FLTAAEGVVT IDTTDLSVDE VLERVLALVD AARGIEAPAV PGPTADADAA
ATGMPGATGV DDEAVEAAWR AGLEDYALDE EDLALLAGDE EELPRGAERA PLPVLAVVGR
PNVGKSTLVN RILGRREAVV EDVPGVTRDR VFYEAEWSGT DFWLVDTGGW EDRVQGIAYR
VAEQAELAVE LADVVLFVVD ANVGITATDE QLLKVLRRAK RPIILCANKV DDERGELEAA
ALWNLGLGEP HPVSALHGRG SGDLLDAVLA VMPEEGRGLP PDSGPRRVAL VGRPNVGKSS
LLNRLAGENR VVVDDEAGTT RDPVDEKIEL GGVPWTFVDT AGIRRRVLQS QGADFYASLR
TRSALDRAEV AVVLLEASET ISTQDLKIID MVLESGRALV LAFNKWDLID EERRAQLERE
IEKDLAHVAW APRVNLSAKT GRHTDKLVPA LNTALDSWDT RIPTGRLNAF LGTLVAAHPH
PLRGGKQSRI LFATQARTRP PRFVIFASGF LEHGYRRFIE RRLREDFGFA GSPIEIGVRI
REKRRR
//
