ID D3FBN7_CONWI Unreviewed; 882 AA.
AC D3FBN7;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Polyphosphate kinase {ECO:0000256|HAMAP-Rule:MF_00347, ECO:0000256|RuleBase:RU003800};
DE EC=2.7.4.1 {ECO:0000256|HAMAP-Rule:MF_00347, ECO:0000256|RuleBase:RU003800};
DE AltName: Full=ATP-polyphosphate phosphotransferase {ECO:0000256|HAMAP-Rule:MF_00347};
DE AltName: Full=Polyphosphoric acid kinase {ECO:0000256|HAMAP-Rule:MF_00347};
GN Name=ppk {ECO:0000256|HAMAP-Rule:MF_00347};
GN OrderedLocusNames=Cwoe_0973 {ECO:0000313|EMBL:ADB49406.1};
OS Conexibacter woesei (strain DSM 14684 / CIP 108061 / JCM 11494 / NBRC
OS 100937 / ID131577).
OC Bacteria; Actinomycetota; Thermoleophilia; Solirubrobacterales;
OC Conexibacteraceae; Conexibacter.
OX NCBI_TaxID=469383 {ECO:0000313|EMBL:ADB49406.1, ECO:0000313|Proteomes:UP000008229};
RN [1] {ECO:0000313|EMBL:ADB49406.1, ECO:0000313|Proteomes:UP000008229}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14684 / CIP 108061 / JCM 11494 / NBRC 100937 / ID131577
RC {ECO:0000313|Proteomes:UP000008229};
RX PubMed=21304704;
RA Pukall R., Lapidus A., Glavina Del Rio T., Copeland A., Tice H.,
RA Cheng J.-F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S.,
RA Mavromatis K., Ivanova N., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.-J., Jeffries C.D., Chain P.,
RA Meincke L., Sims D., Brettin T., Detter J.C., Rohde M., Goeker M.,
RA Bristow J., Eisen J.A., Markowitz V., Kyrpides N.C., Klenk H.-P.,
RA Hugenholtz P.;
RT "Complete genome sequence of Conexibacter woesei type strain (ID131577).";
RL Stand. Genomic Sci. 2:212-219(2010).
RN [2] {ECO:0000313|Proteomes:UP000008229}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14684 / CIP 108061 / JCM 11494 / NBRC 100937 / ID131577
RC {ECO:0000313|Proteomes:UP000008229};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Mikhailova N., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F.,
RA Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA Wu D., Pukall R., Steenblock K., Schneider S., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Conexibacter woesei DSM 14684.";
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible transfer of the terminal phosphate
CC of ATP to form a long-chain polyphosphate (polyP). {ECO:0000256|HAMAP-
CC Rule:MF_00347, ECO:0000256|RuleBase:RU003800}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[phosphate](n) + ATP = [phosphate](n+1) + ADP;
CC Xref=Rhea:RHEA:19573, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14280,
CC ChEBI:CHEBI:16838, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; EC=2.7.4.1;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00347,
CC ECO:0000256|RuleBase:RU003800};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00347};
CC -!- PTM: An intermediate of this reaction is the autophosphorylated ppk in
CC which a phosphate is covalently linked to a histidine residue through a
CC N-P bond. {ECO:0000256|HAMAP-Rule:MF_00347,
CC ECO:0000256|RuleBase:RU003800}.
CC -!- SIMILARITY: Belongs to the polyphosphate kinase 1 (PPK1) family.
CC {ECO:0000256|HAMAP-Rule:MF_00347, ECO:0000256|RuleBase:RU003800}.
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DR EMBL; CP001854; ADB49406.1; -; Genomic_DNA.
DR RefSeq; WP_012932459.1; NC_013739.1.
DR AlphaFoldDB; D3FBN7; -.
DR STRING; 469383.Cwoe_0973; -.
DR KEGG; cwo:Cwoe_0973; -.
DR eggNOG; COG0317; Bacteria.
DR eggNOG; COG0855; Bacteria.
DR HOGENOM; CLU_009678_4_2_11; -.
DR OrthoDB; 9761456at2; -.
DR Proteomes; UP000008229; Chromosome.
DR GO; GO:0009358; C:polyphosphate kinase complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008976; F:polyphosphate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006799; P:polyphosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd09165; PLDc_PaPPK1_C1_like; 1.
DR CDD; cd09168; PLDc_PaPPK1_C2_like; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR Gene3D; 3.30.1840.10; Polyphosphate kinase middle domain; 1.
DR Gene3D; 1.20.58.310; Polyphosphate kinase N-terminal domain; 1.
DR HAMAP; MF_00347; Polyphosphate_kinase; 1.
DR InterPro; IPR003414; PP_kinase.
DR InterPro; IPR041108; PP_kinase_C_1.
DR InterPro; IPR024953; PP_kinase_middle.
DR InterPro; IPR036830; PP_kinase_middle_dom_sf.
DR InterPro; IPR025200; PPK_C_dom2.
DR InterPro; IPR025198; PPK_N_dom.
DR InterPro; IPR036832; PPK_N_dom_sf.
DR NCBIfam; TIGR03705; poly_P_kin; 1.
DR PANTHER; PTHR30218; POLYPHOSPHATE KINASE; 1.
DR PANTHER; PTHR30218:SF0; POLYPHOSPHATE KINASE; 1.
DR Pfam; PF13328; HD_4; 1.
DR Pfam; PF02503; PP_kinase; 1.
DR Pfam; PF13090; PP_kinase_C; 1.
DR Pfam; PF17941; PP_kinase_C_1; 1.
DR Pfam; PF13089; PP_kinase_N; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR SUPFAM; SSF143724; PHP14-like; 1.
DR SUPFAM; SSF140356; PPK N-terminal domain-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00347};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00347};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00347};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00347};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00347};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW Rule:MF_00347}; Reference proteome {ECO:0000313|Proteomes:UP000008229};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00347}.
FT DOMAIN 200..306
FT /note="Polyphosphate kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13089"
FT DOMAIN 315..491
FT /note="Polyphosphate kinase middle"
FT /evidence="ECO:0000259|Pfam:PF02503"
FT DOMAIN 522..687
FT /note="Polyphosphate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17941"
FT DOMAIN 695..856
FT /note="Polyphosphate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13090"
FT ACT_SITE 626
FT /note="Phosphohistidine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00347"
FT BINDING 238
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00347"
FT BINDING 566
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00347"
FT BINDING 596
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00347"
FT BINDING 659
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00347"
FT BINDING 755
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00347"
FT BINDING 783
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00347"
SQ SEQUENCE 882 AA; 97782 MW; 5DB40DB72BFE556F CRC64;
MSSTARSASP TGELPAFARD SDTIASAWAL ALETYRANGG GNIAADVEHV AITARLLHDA
GADDATVATA VLHDLIEDTG VDRSVIAARV GEEIARRVDA LTERPELDSY PERKAELRAR
GIEAGREVAA VMAADKLARA TRAAGGRLRP EKLRHYQATL EQLRDAFPDL PLLGQLGEAI
ERLKPADATK TVETVDPQHF INRELSWLDF NERVLQLAED AHQPLLERAK FCAIYSSNLD
EFFMVRVAGV HDQVDAGIEA TSSDGIPPDE LLRAIAARVQ ELGARQAAVY QEVLLPSLAE
HGIRIVDWDA LDEQEREQLR ARFEREVFPA LTPLAVGPAQ PFPYISNLSL SLAVLVRDPE
TDQTRFARVK VPKEGLPRFV QIGEGARTLV PMESVIAAHL EQLFRGMEIV AHAVFRVTRD
ADFTVSDEAD DLLEAVEAQL RRRRFGEVVR LEVSAGIDPT LRARLAAELS IENSDVYEVA
GLLDYADLWQ VVKLPGFRDL RNAPWTPVMP PEFVEDDKKP ANLFRQLRKR DLLVHHPYDS
FSTVEQFVQQ AVADPKVLAI KQTVYRTSDD SPLVPALIRA AERGKQAVGL VELKARFDER
QNITWARALE QAGVHVTFGM PGLKTHAKAV LVVRREGDGV RHYAHIGTGN YHAGTAHLYT
DFGLFTADDE ITAEIAELFN QLTGYSKPEG YERVLVAPLN LRDRIIEQID LTIAAHTPEQ
PARIAMKMNS LVDSACIRAL YRASQAGVRV ELNVRGACCL RPGVSGVSEN IRVVSIVGRF
LEHSRIYAFQ RDGETSIFMG SADLMPRNLD SRVELVVPVQ DADARAEVLD TLERCLADTE
NAWDLRADGT WTHRRVQPGD ERRDVQAELM RAHLARAEHV EA
//
