ID   A0A3A9NHE7_MORCA        Unreviewed;       715 AA.
AC   A0A3A9NHE7;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   10-APR-2019, entry version 4.
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=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
RT   COPD subjects.";
RL   Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
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:RKL89374.1}.
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DR   EMBL; QZGP01000003; RKL89374.1; -; Genomic_DNA.
DR   RefSeq; WP_064603541.1; NZ_QZGX01000008.1.
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|HAMAP-Rule:MF_00347,
KW   ECO:0000256|SAAS:SAAS00008173};
KW   Complete proteome {ECO:0000313|Proteomes:UP000270318};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00347,
KW   ECO:0000256|SAAS:SAAS00008205, ECO:0000313|EMBL:RKL89374.1};
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:RKL89374.1}.
FT   DOMAIN       38    143       PP_kinase_N. {ECO:0000259|Pfam:PF13089}.
FT   DOMAIN      152    350       PP_kinase. {ECO:0000259|Pfam:PF02503}.
FT   DOMAIN      363    527       PP_kinase_C_1. {ECO:0000259|Pfam:
FT                                PF17941}.
FT   DOMAIN      536    696       PP_kinase_C. {ECO:0000259|Pfam:PF13090}.
FT   ACT_SITE    467    467       Phosphohistidine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00347}.
FT   METAL       407    407       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00347}.
FT   METAL       437    437       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00347}.
FT   BINDING      76     76       ATP. {ECO:0000256|HAMAP-Rule:MF_00347}.
FT   BINDING     500    500       ATP. {ECO:0000256|HAMAP-Rule:MF_00347}.
FT   BINDING     596    596       ATP. {ECO:0000256|HAMAP-Rule:MF_00347}.
FT   BINDING     624    624       ATP. {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
//