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Database: UniProt
Entry: A0A0U5GKG3_9GAMM
LinkDB: A0A0U5GKG3_9GAMM
Original site: A0A0U5GKG3_9GAMM 
ID   A0A0U5GKG3_9GAMM        Unreviewed;      1066 AA.
AC   A0A0U5GKG3;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Chemotaxis protein CheY {ECO:0000256|ARBA:ARBA00040987};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=EM595_1402 {ECO:0000313|EMBL:CUU23636.1};
OS   Duffyella gerundensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Duffyella.
OX   NCBI_TaxID=1619313 {ECO:0000313|EMBL:CUU23636.1, ECO:0000313|Proteomes:UP000059419};
RN   [1] {ECO:0000313|Proteomes:UP000059419}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Blom J.;
RL   Submitted (NOV-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};
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DR   EMBL; LN907827; CUU23636.1; -; Genomic_DNA.
DR   RefSeq; WP_067429513.1; NZ_LN907827.1.
DR   AlphaFoldDB; A0A0U5GKG3; -.
DR   STRING; 1619313.EM595_1402; -.
DR   KEGG; ege:EM595_1402; -.
DR   PATRIC; fig|1619313.3.peg.1452; -.
DR   OrthoDB; 9770795at2; -.
DR   Proteomes; UP000059419; Chromosome 1.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; cd17546; REC_hyHK_CKI1_RcsC-like; 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; 1.20.120.160; HPT domain; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 4.
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; IPR036641; HPT_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
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; PF01627; Hpt; 1.
DR   Pfam; PF00072; Response_reg; 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; SM00062; PBPb; 2.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50894; HPT; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000059419};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..1066
FT                   /note="Chemotaxis protein CheY"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006857969"
FT   DOMAIN          586..804
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          823..943
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          959..1052
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   MOD_RES         873
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         998
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   1066 AA;  118682 MW;  745DFDDEA88907B7 CRC64;
     MIPFFRLLLP LLCLCFGAAA ANNSSLLPRV EVPLPAVTLS AASQQWLATH KVLRVGYWAT
     SQPPISLDRK ADQLEGVSAE FLQLIGASFN RPIRLTRYEN SQQARDALQA GNIDMLAFWS
     TENDRNDGML HSLPWMLDHD LLVQRLSSDP KDDLRQQRLM YVDGSTAPLN LQQRWPKATL
     QAVYSVLEGL LAIRYDSDTL MWGHASVINY FLQQRRFYEL TSREPATPVA TRWTFTARAD
     NDVLINAVNA VLAALPVSSY TAINEYWGMG LEHIPVRVPF ALSPDLQHWI AQHPQINVYF
     ARTHLPLSYI DDEGDISGLS INLLKMIAAR SGLNFNFVPV DNAIALKTAL EQDAQGMLAV
     ADPADSSNRH LLFSRAYMQS PWVLVARKDA PAWRSLADMA GKKVAVYQPL AFVDSLAKRF
     PAVKFVHTDY AFRTVEQLFT GQIDAVVLPE QITSYLLKIY LGDRFRILMP APVSPSDVTF
     ATREHNTPLM EILNQGLLAF PPQALNLQMS QWISDAGPAR LTPWSDYRDY VVQYAPVAAL
     IVLFIFWRNY ILKKNLHERR NNEQALLEAR ERADNANDAK GRFLAQMSHE IRTPLNALVG
     LLDLEQRGLS QPAQHQHNIQ AAADSSRALL LLVGDILDLA KIESGTLQMR PQPVSLTRLT
     EQIITLFRPQ AAEKGITLQY ECELHQPWVL FDALMFKQLL SNLLSNAIKF TDQGEVSVAL
     YQGKSADVAQ GLYMLEVSDS GIGMSAALAQ TIFEPYVQGE TLQKGTGLGL SICRQLAELC
     GATLSVESEP GEGSTFMLRF TAPITTPVER AAPLALSLQL NKRVLIVDDH APSRLLLSQQ
     LELAGCDVTT AEQGEQALCI WHNSAPFDVV ITDCHMPVMD GFTFAQRLRD AERQAQRAPV
     RLLGLTAMAE QHIIERAQQA GMDGCLFKPL ELEELLRQVG NQTAPPQVIA RIQALAKADQ
     HAMQELAAAT RQQNRHDIQR LAAAIAEQDA QAVAQIAHLI AGGARLLHLD SLFHCCQQLE
     TVARHTQWAE IATLYAQLAQ QIEALDLTLQ QQMMTGDEQE PSQNRS
//
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