ID   A0A3A9NHE7_MORCA        Unreviewed;       715 AA.
AC   A0A3A9NHE7;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   25-MAY-2022, entry version 11.
DE   RecName: Full=Polyphosphate kinase {ECO:0000256|HAMAP-Rule:MF_00347, ECO:0000256|RuleBase:RU003800};
DE            EC=2.7.4.1 {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; Moraxellales; Moraxellaceae;
OC   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|HAMAP-Rule:MF_00347,
CC         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}.
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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   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};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00347}.
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          537..695
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
//