ID A0A166MJ74_STAPS Unreviewed; 722 AA. AC A0A166MJ74; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 16-JAN-2019, entry version 24. DE RecName: Full=Polyphosphate kinase {ECO:0000256|HAMAP-Rule:MF_00347, ECO:0000256|RuleBase:RU003800, ECO:0000256|SAAS:SAAS00008280}; DE EC=2.7.4.1 {ECO:0000256|HAMAP-Rule:MF_00347, ECO:0000256|RuleBase:RU003800, ECO:0000256|SAAS:SAAS00008280}; 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 ORFNames=DD902_07530 {ECO:0000313|EMBL:PWZ74647.1}, DV946_05845 GN {ECO:0000313|EMBL:REB27628.1}, DV961_05090 GN {ECO:0000313|EMBL:REA82447.1}; OS Staphylococcus pseudintermedius. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=283734 {ECO:0000313|EMBL:REA82447.1, ECO:0000313|Proteomes:UP000256409}; RN [1] {ECO:0000313|EMBL:PWZ74647.1, ECO:0000313|Proteomes:UP000246800} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ST525 1 {ECO:0000313|EMBL:PWZ74647.1, RC ECO:0000313|Proteomes:UP000246800}; RX PubMed=29292005; RA Worthing K.A., Abraham S., Coombs G.W., Pang S., Saputra S., RA Jordan D., Trott D.J., Norris J.M.; RT "Clonal diversity and geographic distribution of methicillin-resistant RT Staphylococcus pseudintermedius from Australian animals: Discovery of RT novel sequence types."; RL Vet. Microbiol. 213:58-65(2018). RN [2] {ECO:0000313|EMBL:REA82447.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ST496-2 {ECO:0000313|EMBL:REA82447.1}, and ST496-5 RC {ECO:0000313|EMBL:REB27628.1}; RX PubMed=30173756; DOI=.1016/j.vetmic.2018.07.021; RA Worthing K.A., Brown J., Gerber L., Abraham S., Trott D., Norris J.M.; RT "Methicillin-resistant staphylococci amongst veterinary personnel, RT personnel-owned pets, patients and the hospital environment of two RT small animal veterinary hospitals."; RL Vet. Microbiol. 223:79-85(2018). RN [3] {ECO:0000313|Proteomes:UP000256409, ECO:0000313|Proteomes:UP000256583} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ST496-2 {ECO:0000313|Proteomes:UP000256409}, and ST496-5 RC {ECO:0000313|Proteomes:UP000256583}; RA Worthing K.A., Brown J., Gerber L., Abraham S., Trott D., Norris J.M.; RT "Molecular epidemiology of methicillin-resistant staphylococci amongst RT veterinary personnel, personnel-owned pets, patients and the hospital RT environment of two companion animal veterinary hospitals."; RL Vet. Microbiol. 0:0-0(2018). CC -!- FUNCTION: Catalyzes the reversible transfer of the terminal CC phosphate of ATP to form a long-chain polyphosphate (polyP). CC {ECO:0000256|HAMAP-Rule:MF_00347, ECO:0000256|RuleBase:RU003800, CC ECO:0000256|SAAS:SAAS00537780}. 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; CC EC=2.7.4.1; Evidence={ECO:0000256|HAMAP-Rule:MF_00347, CC ECO:0000256|RuleBase:RU003800, ECO:0000256|SAAS:SAAS01115515}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00347}; CC -!- PTM: An intermediate of this reaction is the autophosphorylated CC ppk in which a phosphate is covalently linked to a histidine CC residue through a 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, CC ECO:0000256|SAAS:SAAS00944215}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:REA82447.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; QEIT01000034; PWZ74647.1; -; Genomic_DNA. DR EMBL; QQPC01000028; REA82447.1; -; Genomic_DNA. DR EMBL; QQPH01000042; REB27628.1; -; Genomic_DNA. DR RefSeq; WP_014613536.1; NZ_QQTV01000049.1. DR EnsemblBacteria; ANS89159; ANS89159; A6M57_4205. DR EnsemblBacteria; KZK23826; KZK23826; NO89_11555. DR GeneID; 29755566; -. DR OrthoDB; 76567at2; -. DR Proteomes; UP000246800; Unassembled WGS sequence. DR Proteomes; UP000256409; Unassembled WGS sequence. DR Proteomes; UP000256583; Unassembled WGS sequence. 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:0006799; P:polyphosphate biosynthetic process; IEA:UniProtKB-UniRule. DR Gene3D; 3.30.1840.10; -; 1. DR HAMAP; MF_00347; Polyphosphate_kinase; 1. DR InterPro; IPR003414; PP_kinase. 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 PANTHER; PTHR30218; PTHR30218; 1. DR Pfam; PF02503; PP_kinase; 1. DR Pfam; PF13090; PP_kinase_C; 1. DR Pfam; PF13089; PP_kinase_N; 1. DR PIRSF; PIRSF015589; PP_kinase; 1. DR SUPFAM; SSF140356; SSF140356; 1. DR TIGRFAMs; TIGR03705; poly_P_kin; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00347, KW ECO:0000256|SAAS:SAAS00008173}; KW Complete proteome {ECO:0000313|Proteomes:UP000246800, KW ECO:0000313|Proteomes:UP000256409, ECO:0000313|Proteomes:UP000256583}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00347, KW ECO:0000256|SAAS:SAAS00008205, ECO:0000313|EMBL:REA82447.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00347}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00347}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00347, KW ECO:0000256|SAAS:SAAS00008137}; KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00347, KW ECO:0000256|RuleBase:RU003800}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00347, KW ECO:0000256|RuleBase:RU003800, ECO:0000256|SAAS:SAAS00008215, KW ECO:0000313|EMBL:REA82447.1}. FT DOMAIN 18 123 PP_kinase_N. {ECO:0000259|Pfam:PF13089}. FT DOMAIN 134 330 PP_kinase. {ECO:0000259|Pfam:PF02503}. FT DOMAIN 509 679 PP_kinase_C. {ECO:0000259|Pfam:PF13090}. FT ACT_SITE 441 441 Phosphohistidine intermediate. FT {ECO:0000256|HAMAP-Rule:MF_00347}. FT METAL 381 381 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00347}. FT METAL 411 411 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00347}. FT BINDING 56 56 ATP. {ECO:0000256|HAMAP-Rule:MF_00347}. FT BINDING 474 474 ATP. {ECO:0000256|HAMAP-Rule:MF_00347}. FT BINDING 570 570 ATP. {ECO:0000256|HAMAP-Rule:MF_00347}. FT BINDING 598 598 ATP. {ECO:0000256|HAMAP-Rule:MF_00347}. SQ SEQUENCE 722 AA; 83921 MW; 67F80AF783CA5C1B CRC64; MKVTIEKGSL DLNHPDYYNN REVSWLDFNY RVLQEACDDQ NPLLEQLKFI AIGSANLDEF FMVRVAGLKD QVKMGFNKPE NKAQLTPQQQ LKAIEQKNRQ NVAFQYQRFN TLVETLKTYD VYLCKPDVLN EDMRKQLEQI FLNDILPTLT PLGIDAYRPF PKLNNKTLNI FVDIDTGDEI NSAIVQIPTL LNRFITINEG NRQYIILIED MISFFMGYLF KGYEILNTYT FRITRNADLT IHEDGAEDLL IEIERFLKER KSGAAVRLEI DHREQQEMQI DWLIDTLELE PQDVYYTNGP LDLTMVFELV DHLSHKLKDL KYERYTPQVP QSLGNDNVYD LALKRDIFFH HPYESFDPIV DFITEASEDP DTLAIKQTLY RVSSDSPIIE ALKNAAENGK QVTVLVELKA RFDEENNVHW AKMLEEAGCH VMYGMTHLKT HSKITLVVKR VNGKLVPFVH LGTGNYNDKT AKLYTDMGII TTNREIGEDA MNFFNYLSGY SMKPDYQQLI VAPYEIRDLF IERIDEEIES HRQHGNGKMM MKMNSLTDKA LIKKLYEASQ AGVQVKLIIR GICCLKPGIP GISDNIEVVS IVGRLLEHSR IYYFYNNGKE KIYLSSADMM TRNMIKRVEI LFPILDKRIA RRLVDFMHLQ LSDNQKGRYQ DASGVYHYVK NELAPINSQE YLMREAQEYG LALSKQNMIE TGQPVRAKRN WMDRVKGHLK RK //