ID A0A166MJ74_STAPS Unreviewed; 722 AA. AC A0A166MJ74; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 10-FEB-2021, entry version 35. DE RecName: Full=Polyphosphate kinase {ECO:0000256|ARBA:ARBA00012960, ECO:0000256|HAMAP-Rule:MF_00347, ECO:0000256|RuleBase:RU003800}; DE EC=2.7.4.1 {ECO:0000256|ARBA:ARBA00012960, 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 ORFNames=DD902_07530 {ECO:0000313|EMBL:PWZ74647.1}, DV961_05090 GN {ECO:0000313|EMBL:REA82447.1}, GB868_11125 GN {ECO:0000313|EMBL:MRI06635.1}; 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; DOI=10.1016/j.vetmic.2017.11.018; RA Worthing K.A., Abraham S., Coombs G.W., Pang S., Saputra S., Jordan D., RA Trott D.J., Norris J.M.; RT "Clonal diversity and geographic distribution of methicillin-resistant RT Staphylococcus pseudintermedius from Australian animals: Discovery of novel RT 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}; RX PubMed=30173756; DOI=10.1016/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 small RT animal veterinary hospitals."; RL Vet. Microbiol. 223:79-85(2018). RN [3] {ECO:0000313|Proteomes:UP000256409} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ST496-2 {ECO:0000313|Proteomes:UP000256409}; 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). RN [4] {ECO:0000313|EMBL:MRI06635.1, ECO:0000313|Proteomes:UP000430957} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=625 {ECO:0000313|EMBL:MRI06635.1, RC ECO:0000313|Proteomes:UP000430957}; RA Zeman M.; RT "New genus Fibralongavirus in Staphylococcus pseudintermedius Siphoviridae RT phages."; RL Submitted (OCT-2019) 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|ARBA:ARBA00000848, ECO:0000256|HAMAP- CC Rule:MF_00347, 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}. 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: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; WJOJ01000023; MRI06635.1; -; Genomic_DNA. DR EMBL; QEIT01000034; PWZ74647.1; -; Genomic_DNA. DR EMBL; QQPC01000028; REA82447.1; -; Genomic_DNA. DR RefSeq; WP_014613536.1; NZ_WWPQ01000059.1. DR STRING; 984892.SPSE_0950; -. DR EnsemblBacteria; ANS89159; ANS89159; A6M57_4205. DR EnsemblBacteria; KZK23826; KZK23826; NO89_11555. DR GeneID; 29755566; -. DR eggNOG; COG0855; Bacteria. DR OrthoDB; 76567at2; -. DR Proteomes; UP000246800; Unassembled WGS sequence. DR Proteomes; UP000256409; Unassembled WGS sequence. DR Proteomes; UP000430957; 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; 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 PANTHER; PTHR30218; PTHR30218; 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 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|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00347}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00347, KW ECO:0000313|EMBL:REA82447.1}; 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, ECO:0000256|RuleBase:RU003800}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00347, ECO:0000256|RuleBase:RU003800, ECO:0000313|EMBL:REA82447.1}. FT DOMAIN 18..123 FT /note="PP_kinase_N" FT /evidence="ECO:0000259|Pfam:PF13089" FT DOMAIN 134..330 FT /note="PP_kinase" FT /evidence="ECO:0000259|Pfam:PF02503" FT DOMAIN 339..501 FT /note="PP_kinase_C_1" FT /evidence="ECO:0000259|Pfam:PF17941" FT DOMAIN 509..679 FT /note="PP_kinase_C" FT /evidence="ECO:0000259|Pfam:PF13090" FT ACT_SITE 441 FT /note="Phosphohistidine intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00347" FT METAL 381 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00347" FT METAL 411 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00347" FT BINDING 56 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00347" FT BINDING 474 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00347" FT BINDING 570 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00347" FT BINDING 598 FT /note="ATP" FT /evidence="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 //