ID A0A3A9NHE7_MORCA Unreviewed; 715 AA. AC A0A3A9NHE7; DT 05-DEC-2018, integrated into UniProtKB/TrEMBL. DT 05-DEC-2018, sequence version 1. DT 07-APR-2021, entry version 8. 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=ppk1 {ECO:0000313|EMBL:RKL89374.1}; GN Synonyms=ppk {ECO:0000256|HAMAP-Rule:MF_00347}; GN ORFNames=D6D77_03485 {ECO:0000313|EMBL:RKL89374.1}; OS Moraxella catarrhalis (Branhamella catarrhalis). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Moraxella. OX NCBI_TaxID=480 {ECO:0000313|EMBL:RKL89374.1, ECO:0000313|Proteomes:UP000270318}; RN [1] {ECO:0000313|EMBL:RKL89374.1, ECO:0000313|Proteomes:UP000270318} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=COPD_M112 {ECO:0000313|EMBL:RKL89374.1, RC ECO:0000313|Proteomes:UP000270318}; RA George L., Haigh R., Mistry V., Haldar K., Barer M., Oggioni M., RA Brightling C.; RT "Sputum M. catarrhalis strains exhibit diversity within and between COPD RT subjects."; RL Submitted (SEP-2018) 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:RKL89374.1}. 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; QZGP01000003; RKL89374.1; -; Genomic_DNA. DR RefSeq; WP_064603541.1; NZ_QZGX01000008.1. DR EnsemblBacteria; RKL89374; RKL89374; D6D77_03485. DR Proteomes; UP000270318; 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:RKL89374.1}; 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:RKL89374.1}. FT DOMAIN 38..143 FT /note="PP_kinase_N" FT /evidence="ECO:0000259|Pfam:PF13089" FT DOMAIN 152..350 FT /note="PP_kinase" FT /evidence="ECO:0000259|Pfam:PF02503" FT DOMAIN 363..527 FT /note="PP_kinase_C_1" FT /evidence="ECO:0000259|Pfam:PF17941" FT DOMAIN 536..696 FT /note="PP_kinase_C" FT /evidence="ECO:0000259|Pfam:PF13090" FT ACT_SITE 467 FT /note="Phosphohistidine intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00347" FT METAL 407 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00347" FT METAL 437 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00347" FT BINDING 76 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00347" FT BINDING 500 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00347" FT BINDING 596 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00347" FT BINDING 624 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00347" SQ SEQUENCE 715 AA; 80779 MW; 2BF70EABBFD36DC1 CRC64; MINTMNDVNQ ANHADHTNPM TQIDHLFDEK GAFTPKCYIN RDLSALRFQL RVLAQAANPN HPLLERMFFL TIFSSNLDEF FEIRVAGLLQ KMKQGDQVSS LDGRKPSEIL QIISDIAHGA VTQQYQILND EILPELAKHE IRYLRRDELN AKQRAWLKDY FVSQVKPVLT PISIDPAHPF PRLVNKSLNF IISLEGKDAF GRDINRAIVP APRSLPRVIR LPDEITDGKE HHVMLSAVIH EHINELFLGM KVTGCYQFRL TRNADLALAD DVDDIAKALE GELDNRRFGH EVRLEVTTNC PQDICDFLLD EFELDKSQLY RVNGPVNLTR LLTSFDRPEL KFKPFTPAMP KAFRDMDMSS AGSMFAAISR QDVLVHHPFH TFNPVINLLW QAASDPNVLA IKQTIYRSGV NSEIVQALAA AARSGKEVTA VIELRARFDE ASNIAVANML QEAGAVVVYG IVGYKTHAKM MLIVRRENGK IRRYVHLGTG NYHAGNAKAY TDYGLFTANA EVTEDVAGVF QQLTGMGRPL PSKQILHAPF TLHDTLMRLI DHEIAHVKAG KKGRIIMKFN ALTERKIINK LYEASIAGVQ IDLIVRSICC LRPQVAGLSE NIRVRSIVGR FLEHTRVYYF ANGGEERLYC SSADLMDRNL LHRVEVAFPI LDKKIFKKIY EDGLMNYLKD DVQAWELLGD GKWQPLLASG GTHDAQKTLL EKITL //