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Database: UniProt
Entry: Q815A6_BACCR
LinkDB: Q815A6_BACCR
Original site: Q815A6_BACCR 
ID   Q815A6_BACCR            Unreviewed;       476 AA.
AC   Q815A6;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 133.
DE   RecName: Full=Histidine protein kinase SaeS {ECO:0000256|ARBA:ARBA00044126};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE   AltName: Full=Sensor protein SaeS {ECO:0000256|ARBA:ARBA00044288};
DE   AltName: Full=Staphylococcus exoprotein expression protein S {ECO:0000256|ARBA:ARBA00044353};
GN   OrderedLocusNames=BC_5261 {ECO:0000313|EMBL:AAP12125.1};
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900 {ECO:0000313|EMBL:AAP12125.1, ECO:0000313|Proteomes:UP000001417};
RN   [1] {ECO:0000313|EMBL:AAP12125.1, ECO:0000313|Proteomes:UP000001417}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB
RC   9373 / NCTC 2599 / NRRL B-3711 {ECO:0000313|Proteomes:UP000001417};
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
CC   -!- FUNCTION: Member of the two-component regulatory system SaeR/SaeS
CC       involved in the regulation of staphylococcal virulence factors in a
CC       strain-dependent fashion. Probably functions as a membrane-associated
CC       protein kinase that upon sensing the appropriate signal,
CC       autophosphorylates and in turn activates the cytosolic response
CC       regulator SaeR. {ECO:0000256|ARBA:ARBA00043865}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; AE016877; AAP12125.1; -; Genomic_DNA.
DR   RefSeq; NP_834924.1; NC_004722.1.
DR   RefSeq; WP_000054029.1; NZ_CP034551.1.
DR   AlphaFoldDB; Q815A6; -.
DR   KEGG; bce:BC5261; -.
DR   PATRIC; fig|226900.8.peg.5431; -.
DR   HOGENOM; CLU_000445_89_6_9; -.
DR   OrthoDB; 9786919at2; -.
DR   Proteomes; UP000001417; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IBA:GO_Central.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   PANTHER; PTHR45528:SF13; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR45528; SENSOR HISTIDINE KINASE CPXA; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AAP12125.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001417};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AAP12125.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        7..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          187..239
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          254..464
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   476 AA;  53614 MW;  AC67849FCA472428 CRC64;
     MSLKRNMVFG IVGLLIPIFV LLYAVVYITL EKNMYHNAAD SLEKLSVEAQ IYTMNYLEKE
     AEVDTLGPNS LLIASYLAKR MDVRVQMIGK NGDVVADTQK GALLHRNIDI ESSLKGKKSY
     VFEEADPAPI LLFSSPVYYG NDVIGSIRFI NELTGEKEVL TNVSWTFLMT SLCLVATGIF
     FAIRLAKSLH KPIDQLRQMA QRLANGDYKS KIELNEYVEI AQLSASFNAM ADGIELHIKQ
     LQEEKEKQKD FLDRITHELK TPLTAIIGYV DLIPKLQSKE DVQESLRYVS VESERLLSLV
     EELLKSSKYG KSTFEVSPTV VNIKELAEEA VSIVKPRLNQ FEIEVINELT DVHVVADFDK
     TKQIFLNVLD NAIKYSDASH IRMNVIVNEH EAKVFVHDDG IGIDEVVLAE WNESPKGKAL
     PSSYGNGYGL YICQEIMSKQ GGSMRIESSE EVGTTIFITF LLPRRMEDIK NLKAVK
//
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