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Database: UniProt
Entry: A0A0Q0B4Z3_PSESX
LinkDB: A0A0Q0B4Z3_PSESX
Original site: A0A0Q0B4Z3_PSESX 
ID   A0A0Q0B4Z3_PSESX        Unreviewed;      1015 AA.
AC   A0A0Q0B4Z3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=ALO94_01290 {ECO:0000313|EMBL:KPY69790.1};
OS   Pseudomonas syringae pv. spinaceae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=264459 {ECO:0000313|EMBL:KPY69790.1, ECO:0000313|Proteomes:UP000050384};
RN   [1] {ECO:0000313|EMBL:KPY69790.1, ECO:0000313|Proteomes:UP000050384}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICMP16929 {ECO:0000313|EMBL:KPY69790.1,
RC   ECO:0000313|Proteomes:UP000050384};
RA   Thakur S., Wang P.W., Gong Y., Weir B.S., Guttman D.S.;
RT   "Genome announcement of multiple Pseudomonas syringae strains.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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   -!- 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:KPY69790.1}.
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DR   EMBL; LJRI01001209; KPY69790.1; -; Genomic_DNA.
DR   RefSeq; WP_057428095.1; NZ_RBTF01000269.1.
DR   AlphaFoldDB; A0A0Q0B4Z3; -.
DR   PATRIC; fig|264459.3.peg.2378; -.
DR   Proteomes; UP000050384; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   CDD; cd13705; PBP2_BvgS_D1; 1.
DR   CDD; cd13707; PBP2_BvgS_D2; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 5.
DR   InterPro; IPR011006; CheY-like_superfamily.
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   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR001638; Solute-binding_3/MltF_N.
DR   PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF00497; SBP_bac_3; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 1.
DR   SMART; SM00062; PBPb; 2.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 2.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        492..513
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          531..577
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          675..898
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          920..1015
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         969
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1015 AA;  112380 MW;  2105413640F60BCB CRC64;
     MSWSSAQAGP GAADHYTLLG RSSPAHMDVK LDSSQWQWVR AQRELILGTS SPDYPPFDIT
     ISGTDYEGIT ADYAGIISDA LDLPVRVQRF DSREAAMKAL IAGQVDLLGT ANGFEAVERD
     IKLSQPYSVD QPVLVTRVGD TRPLNEGLQG MRLSMVYHYL PPADVVTTYP GAILKTYPSF
     QNAINAVAFN QADVFLGDTI STQYIINKGY LNNVQMSSFG KHEANGFSFA VSGQNTQLLG
     VINQTLKAIP VDERIDISRR WSTGSDLMLT DQKLQLTQRE ERWIAQHPVV RVVVNEAYAP
     LTFFDAKGNF RGITADLLEL VRLRTGLKFD VKRSPSLTDM QNQVSEGQAD MIGALVSSDV
     REDRLSFSRP YIDNSFVLVT RKYPRVVPLE IDNPFQALDM LAVGRTEGAV VSLLSADYFL
     SSGIFEERLQ MTATVGEDPA LISMATSRNA LELSSILDKA LASIAPQDLA AINNRWRAYT
     PSSASWHDYQ RLIYQIVIGA GLLLLGLLVW NAWMRRQIRQ REAAERALSD QYEFMRALVD
     GTPHPIYVRD RDGLLQMCND SYLRAFSAQR EDIIGKSATE GVLGNAFEAR EYAADYQRVM
     ASNTALILDR PLHIGDRQLT IYHWILPFRD SLGEVQGIIG GWIDISDRRQ LIEDLQAAKE
     QADAASRAKS TFLATMSHEI RTPMNAVIGM LELALKRADQ GELDRSAIEV AYSSANDLLD
     LIGDILDIAR IESGRLALNP ERANLRQLVE SVLRVFDGLA RQKDLDLVLE LDSRINTDVL
     IDPLRFKQIL SNLVSNAIKF TPMGRVKIAL QAVDNPDPQL LHLHITVQDS GIGISVEDQK
     RLFEPFAQAD NTGQMARTGA GLGLVICRSL CMMMGGNLSL DSEPGNGTRI SMNLLLTTLE
     PMTRQPVATK PPEAAHQVLR ILIVDDHPAN RLLLCQQLGF LGHHCEMAEN GAQGLERWKA
     DAFDLVVADW NNPVNPKSPY KINTLANKNI IFKVVLADFA APIKSDAYGC VLGKI
//
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