ID   ACKA2_NEIMB             Reviewed;         399 AA.
AC   Q9K0X1;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   16-JUN-2009, entry version 44.
DE   RecName: Full=Acetate kinase 2;
DE            EC=2.7.2.1;
DE   AltName: Full=Acetokinase 2;
GN   Name=ackA2; OrderedLocusNames=NMB0435;
OS   Neisseria meningitidis serogroup B.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Neisseriaceae; Neisseria.
OX   NCBI_TaxID=491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58 / Serogroup B;
RX   MEDLINE=20175755; PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C.,
RA   Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F.,
RA   Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D.,
RA   Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D.,
RA   Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E.,
RA   Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M.,
RA   Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M.,
RA   Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R.,
RA   Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(2000).
CC   -!- CATALYTIC ACTIVITY: ATP + acetate = ADP + acetyl phosphate.
CC   -!- CATALYTIC ACTIVITY: ATP + propanoate = ADP + propanoyl phosphate.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA
CC       biosynthesis; acetyl-CoA from acetate: step 1/2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the acetokinase family.
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DR   EMBL; AE002098; AAF40873.1; -; Genomic_DNA.
DR   PIR; D81198; D81198.
DR   RefSeq; NP_273483.1; -.
DR   HSSP; P38502; 1G99.
DR   GeneID; 902551; -.
DR   GenomeReviews; AE002098_GR; NMB0435.
DR   KEGG; nme:NMB0435; -.
DR   NMPDR; fig|122586.1.peg.417; -.
DR   TIGR; NMB0435; -.
DR   HOGENOM; Q9K0X1; -.
DR   OMA; Q9K0X1; DEGHEGA.
DR   BioCyc; NMEN122586:NMB_0435-MON; -.
DR   BRENDA; 2.7.2.1; 293828.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008776; F:acetate kinase activity; IEA:HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006082; P:organic acid metabolic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:HAMAP.
DR   HAMAP; MF_00020; -; 1.
DR   InterPro; IPR000890; Acetate_kin.
DR   InterPro; IPR004372; AckA.
DR   PANTHER; PTHR21060; Acetate_kin; 1.
DR   PANTHER; PTHR21060:SF11; AckA; 1.
DR   Pfam; PF00871; Acetate_kinase; 1.
DR   PIRSF; PIRSF000722; Acetate_prop_kin; 1.
DR   PRINTS; PR00471; ACETATEKNASE.
DR   TIGRFAMs; TIGR00016; ackA; 1.
DR   PROSITE; PS01075; ACETATE_KINASE_1; 1.
DR   PROSITE; PS01076; ACETATE_KINASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN         1    399       Acetate kinase 2.
FT                                /FTId=PRO_0000107593.
SQ   SEQUENCE   399 AA;  42795 MW;  B672CDD77F8B7A78 CRC64;
     MSDQLILVLN CGSSSLKGAV IDRKSGSVVL SCLGERLTTP EAVITFNKDG NKRQVPLSGR
     NCHAGAVGML LNELEKHGLH DRIKAIGHRI AHGGEKYSES VLIDQAVMDE LNACIPLAPL
     HNPANISGIL AAQEHFPGLP NVGVMDTSFH QTMPERAYTY AVPRELRKKY AFRRYGFHGT
     SMRYVAPEAA RILGKPLEDI RMIIAHLGNG ASITAIKNGK SVDTSMGFTP IEGLVMGTRC
     GDIDPGVYSY LTSHAGMDVA QVDEMLNKKS GLLGISELSN DCRTLEIAAD EGHEGARLAL
     EVMTYRLAKY IASMAVGCGG VDALVFTGGI GENSRNIRAK TVSYLDFLGL HIDTKANMEK
     RYGNSGIISP TDSSPAVLVV PTNEELMIAC DTAELAGIL
//