ID A0A097R8F0_HAFAL Unreviewed; 1185 AA.
AC A0A097R8F0;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Chemotaxis protein CheY {ECO:0000256|ARBA:ARBA00040987};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AT03_19090 {ECO:0000313|EMBL:AIU74974.1};
OS Hafnia alvei FB1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Hafnia.
OX NCBI_TaxID=1453496 {ECO:0000313|EMBL:AIU74974.1, ECO:0000313|Proteomes:UP000029986};
RN [1] {ECO:0000313|EMBL:AIU74974.1, ECO:0000313|Proteomes:UP000029986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FB1 {ECO:0000313|EMBL:AIU74974.1,
RC ECO:0000313|Proteomes:UP000029986};
RX PubMed=25075225; DOI=10.1186/1757-4749-6-29;
RA Tan J.Y., Yin W.F., Chan K.G.;
RT "Gene clusters of Hafnia alvei strain FB1 important in survival and
RT pathogenesis: a draft genome perspective.";
RL Gut Pathog. 6:29-29(2014).
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; CP009706; AIU74974.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A097R8F0; -.
DR KEGG; hav:AT03_19090; -.
DR PATRIC; fig|1453496.5.peg.3927; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG0834; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_37_3_6; -.
DR Proteomes; UP000029986; Chromosome.
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; cd00088; HPT; 1.
DR CDD; cd13705; PBP2_BvgS_D1; 1.
DR CDD; cd13707; PBP2_BvgS_D2; 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; IPR035965; PAS-like_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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AIU74974.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000029986};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000313|EMBL:AIU74974.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 525..546
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 708..928
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 950..1064
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1088..1182
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 999
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1127
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1185 AA; 131906 MW; 91064D4CBABAB201 CRC64;
MGTLFVAQGA IAGKEPIRLE IFSNSGPMLP NLKLSTAEQL WLAKKKTLVV AVYSPESPPL
MLDSSSGRFR GMNAEYLSLL QRALGINVKI DRYESEEFAL NAVKTGKADL VLTSLRTNFN
AVAPFIASLP MVSAYPALVT TQKNVMQPLH TDSPVTIAIA EGYPSEQFVK ASFPNAKILH
YETAYQALAS LYNGKSNYFI GNNLASGTTI MRDFHQSLSI IKFWRTSPIH NQFIALDTQS
PLIPIINNFL AGLTNPITNH ISQPWLESGN PALLTKPLSL TPQEQRWLEK HPKLKVLINP
YYAPFTLLDE NNEIRGVTGD ILNLIHLQTG LEFETVTANS NTEMVDKMLN GDWNILPTAT
YSPSREELIS FTHPIITTPF AIVVRTSSGK AELLPGMKVA VTTMHILTEK LHTKYPGIDL
VQVENTSIGL NLLAEGKVDA VISTQLTARY MIDHYYPNQL KYEIMADEAP ALVSFAIPRG
DQELKQILNK ALDNIPPKSI LFISSKWVKL PDIKIDTWHL YNKQFYIVIT LSIFIILSFL
LWGGYLSREV RMRKQSQADL ENQLSFRKTL SNSIPIPVYT ISLDGEVQSY NSAFMSFFST
DQKNVTSTSL FDSRNPLSDI FSVLNRDIQH GLIPDKVIEH SIMLNNGRED RHIIHWITLC
VMPSDNVMPT LICGWQDVTE SRQLLSALQT EKDKAIQANE AKSTFLASMS HEIRTPVSAV
MGFLELLALH NQSPEEDKES ISLAYATAQS LLGLIGDILD MNKIESGSFE LSPDWVNLDV
LITTVMRGFE GLAKQKQLKL TFVNRLVKGE YLRLDPQATK QLLSNLLSNA IKFTEHGGVE
VSAESIATRS GQTQLILRVT DTGAGISQED QERLFKPYSQ TETGKRQTGS GLGLLICREL
VTRMNGKLGL VSQVGQGTTM TIDLVTAVSH EAMISSVELQ PAVYPAKKLK ILIVDDHPVN
RLLLRRQLDT LGYKVDEASD GNDALILINE NSYDLVITDV NMPNMDGVTL TRHIRSFDSD
IVIWGLTANA QTQEKDRCLA IGMNACLFKP INLQQLASAL ASVGTINMTY QLDEIIDIAT
LRSLALNDPK LMQQMLEQSQ QENNKDFLAA QEAKMAGDWT AFKMHMHRIN GTAQILGAAK
LQELAEKLEN YLVVQTDDSA IEHGMKLLEV ELNRLREAIN SFSPT
//
