ID A0A166MJ74_STAPS Unreviewed; 722 AA. AC A0A166MJ74; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 05-OCT-2016, entry version 3. DE RecName: Full=Polyphosphate kinase {ECO:0000256|HAMAP-Rule:MF_00347, ECO:0000256|RuleBase:RU003800, ECO:0000256|SAAS:SAAS00008191}; DE EC=2.7.4.1 {ECO:0000256|HAMAP-Rule:MF_00347, ECO:0000256|RuleBase:RU003800, ECO:0000256|SAAS:SAAS00008191}; 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=NO87_02950 {ECO:0000313|EMBL:KZK21845.1}, NO88_11380 GN {ECO:0000313|EMBL:KZK17959.1}, NO89_11555 GN {ECO:0000313|EMBL:KZK23826.1}; OS Staphylococcus pseudintermedius. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=283734 {ECO:0000313|EMBL:KZK17959.1}; RN [1] {ECO:0000313|EMBL:KZK17959.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=2001-08-299-1 {ECO:0000313|EMBL:KZK21845.1}, 9841787-1 RC {ECO:0000313|EMBL:KZK23826.1}, and 9841998-1 RC {ECO:0000313|EMBL:KZK17959.1}; RA de Vries L.E., Hasman H., Rabadan S.J., Agersoe Y.; RT "Sequence-based characterization of Tn5801-like genomic islands in RT tetracycline-resistant Staphylococcus pseudintermedius and other Gram- RT positive bacteria from humans and animals."; RL Front. Microbiol. 7:0-0(2016). 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: ATP + (phosphate)(n) = ADP + (phosphate)(n+1). CC {ECO:0000256|HAMAP-Rule:MF_00347, ECO:0000256|RuleBase:RU003800, CC ECO:0000256|SAAS:SAAS00008139}. CC -!- PTM: An intermediate of this reaction is the autophosphorylated CC ppk in which a phosphate is covalently linked to histidine CC residues through a N-P bond. {ECO:0000256|HAMAP-Rule:MF_00347, CC ECO:0000256|RuleBase:RU003800}. CC -!- SIMILARITY: Belongs to the polyphosphate kinase family. CC {ECO:0000256|HAMAP-Rule:MF_00347, ECO:0000256|RuleBase:RU003800, CC ECO:0000256|SAAS:SAAS00537783}. CC -!- SIMILARITY: Contains 1 PLD phosphodiesterase domain. CC {ECO:0000256|HAMAP-Rule:MF_00347}. 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:KZK17959.1}. 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; JTKP01000035; KZK17959.1; -; Genomic_DNA. DR EMBL; JTKO01000001; KZK21845.1; -; Genomic_DNA. DR EMBL; JTKQ01000026; KZK23826.1; -; Genomic_DNA. DR RefSeq; WP_014613536.1; NZ_JTKQ01000026.1. DR GO; GO:0009358; C:polyphosphate kinase complex; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008976; F:polyphosphate kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006799; P:polyphosphate biosynthetic process; IEA:UniProtKB-HAMAP. 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; IPR025200; PPK_C_dom. DR InterPro; IPR025198; PPK_N_dom. 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:SAAS00420136}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00347, KW ECO:0000256|SAAS:SAAS00420135, ECO:0000313|EMBL:KZK17959.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00347, KW ECO:0000256|SAAS:SAAS00420142}; 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:SAAS00420138}. FT DOMAIN 18 123 PP_kinase_N. {ECO:0000259|Pfam:PF13089}. FT DOMAIN 134 330 PP_kinase. {ECO:0000259|Pfam:PF02503}. FT DOMAIN 344 683 PP_kinase_C. {ECO:0000259|Pfam:PF13090}. FT ACT_SITE 441 441 Phosphohistidine intermediate. FT {ECO:0000256|HAMAP-Rule:MF_00347}. FT ACT_SITE 460 460 Phosphohistidine intermediate. FT {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 //