(data stored in ACNUC7421 zone)

SWISSPROT: A0A0H2ZKP1_PSEAB

ID   A0A0H2ZKP1_PSEAB        Unreviewed;       324 AA.
AC   A0A0H2ZKP1;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   07-JUN-2017, entry version 12.
DE   RecName: Full=Stress response kinase A {ECO:0000256|HAMAP-Rule:MF_01497};
DE            EC=2.7.11.1 {ECO:0000256|HAMAP-Rule:MF_01497};
DE   AltName: Full=Serine/threonine-protein kinase SrkA {ECO:0000256|HAMAP-Rule:MF_01497};
GN   Name=srkA {ECO:0000256|HAMAP-Rule:MF_01497};
GN   OrderedLocusNames=PA14_06330 {ECO:0000313|EMBL:ABJ15451.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ15451.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ15451.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ15451.1,
RC   ECO:0000313|Proteomes:UP000000653};
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
CC   -!- FUNCTION: A protein kinase that phosphorylates Ser and Thr
CC       residues. Probably acts to suppress the effects of stress linked
CC       to accumulation of reactive oxygen species. Probably involved in
CC       the extracytoplasmic stress response. {ECO:0000256|HAMAP-
CC       Rule:MF_01497}.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC       {ECO:0000256|HAMAP-Rule:MF_01497}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01497};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01497}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01497}.
CC   -!- SIMILARITY: Belongs to the SrkA/RdoA protein kinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01497}.
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DR   EMBL; CP000438; ABJ15451.1; -; Genomic_DNA.
DR   RefSeq; WP_003129062.1; NC_008463.1.
DR   EnsemblBacteria; ABJ15451; ABJ15451; PA14_06330.
DR   KEGG; pau:PA14_06330; -.
DR   OMA; LIHYSAW; -.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006950; P:response to stress; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_01497; SrkA_kinase; 1.
DR   InterPro; IPR002575; Aminoglycoside_PTrfase.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR032882; SrkA/RdoA.
DR   PANTHER; PTHR39573; PTHR39573; 1.
DR   Pfam; PF01636; APH; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0H2ZKP1.
DR   SWISS-2DPAGE; A0A0H2ZKP1.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01497};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000653};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01497};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_01497, ECO:0000313|EMBL:ABJ15451.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01497};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01497};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01497};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_01497};
KW   Serine/threonine-protein kinase {ECO:0000256|HAMAP-Rule:MF_01497};
KW   Stress response {ECO:0000256|HAMAP-Rule:MF_01497};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01497}.
FT   DOMAIN       32    260       APH. {ECO:0000259|Pfam:PF01636}.
FT   ACT_SITE    199    199       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01497}.
FT   ACT_SITE    216    216       {ECO:0000256|HAMAP-Rule:MF_01497}.
FT   METAL       204    204       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01497}.
FT   METAL       216    216       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01497}.
FT   SITE         33     33       ATP. {ECO:0000256|HAMAP-Rule:MF_01497}.
SQ   SEQUENCE   324 AA;  36967 MW;  0B4AC29382C72127 CRC64;
     MSHPFDQLTP DLVLDAVESL GYLSDARVLA LNSYENRVYQ VGIEDGEPLI AKFYRPDRWS
     DAAIREEHAF SAELAECEVP VVAPLSRDGE SLFAFAGFRF ALFPRRGGRA PEPGNLDQLY
     RLGQLLGRLH AVGATRPFEH REALAVDNFG HASLATLLEG NFIPRSLLPA YESVARDLLK
     RLDALFAEVP YQPIRLHGDC HPGNLLCRDE VYHMVDLDDC RMGPALQDLW MMLAGERHER
     LAQIAELVDG YNEFHDFDPR QLPLLEGLRS LRLMHYSAWL ARRWDDPAFP PSFPWFGSER
     YWGEQVLVLR EQLAALDEEP LRLF
//

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