(data stored in ACNUC7421 zone)

SWISSPROT: Q3ILM5_PSEHT

ID   Q3ILM5_PSEHT            Unreviewed;       324 AA.
AC   Q3ILM5;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 78.
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=rdoA {ECO:0000313|EMBL:CAI85350.1};
GN   Synonyms=srkA {ECO:0000256|HAMAP-Rule:MF_01497};
GN   OrderedLocusNames=PSHAa0247 {ECO:0000313|EMBL:CAI85350.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85350.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85350.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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; CR954246; CAI85350.1; -; Genomic_DNA.
DR   RefSeq; WP_011326964.1; NC_007481.1.
DR   ProteinModelPortal; Q3ILM5; -.
DR   STRING; 326442.PSHAa0247; -.
DR   EnsemblBacteria; CAI85350; CAI85350; PSHAa0247.
DR   KEGG; pha:PSHAa0247; -.
DR   PATRIC; fig|326442.8.peg.238; -.
DR   eggNOG; ENOG4105E27; Bacteria.
DR   eggNOG; COG2334; LUCA.
DR   HOGENOM; HOG000265894; -.
DR   OMA; LIHYSAW; -.
DR   OrthoDB; POG091H04I3; -.
DR   Proteomes; UP000006843; Chromosome I.
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; Q3ILM5.
DR   SWISS-2DPAGE; Q3ILM5.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01497};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01497};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_01497};
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   Reference proteome {ECO:0000313|Proteomes:UP000006843};
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       34    258       APH. {ECO:0000259|Pfam:PF01636}.
FT   ACT_SITE    198    198       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01497}.
FT   ACT_SITE    215    215       {ECO:0000256|HAMAP-Rule:MF_01497}.
FT   METAL       203    203       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01497}.
FT   METAL       215    215       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01497}.
FT   SITE         34     34       ATP. {ECO:0000256|HAMAP-Rule:MF_01497}.
SQ   SEQUENCE   324 AA;  37402 MW;  93362E1548D77729 CRC64;
     MSKFSFIDLT PDLILDAIES VGIYVESGLL ALNSYENRVY QFVAEGGKRY VVKFYRPERW
     SEKQIQEEHD FAFELAEAEV PVVAPMEYNG QSLFEHQGYL FTLFPSVGGR LFEVDNLDQL
     DVLGRLIGRM HQVAKTKPFT QRPTLTCEEY LHTAKVHLQK SNLVPMGLET AFYTILDLVI
     KQAQAQYTNV KTIRLHGDCH AGNILWAGDA LMFVDLDDSR QGPPIQDLWM MLSGDRQTQL
     LQLDTLVTAY EEFCDFDHSQ LKLIEPLRAM RIIHYMGWVA KRWSDPAFVR NFSWFADDKY
     WEQQILALKE QLAALQEAPL KLLP
//

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