ID A0Y9Q4_9GAMM Unreviewed; 2031 AA.
AC A0Y9Q4;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=GP2143_16421 {ECO:0000313|EMBL:EAW32858.1};
OS marine gamma proteobacterium HTCC2143.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Spongiibacteraceae; BD1-7 clade.
OX NCBI_TaxID=247633 {ECO:0000313|EMBL:EAW32858.1, ECO:0000313|Proteomes:UP000004931};
RN [1] {ECO:0000313|EMBL:EAW32858.1, ECO:0000313|Proteomes:UP000004931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2143 {ECO:0000313|EMBL:EAW32858.1,
RC ECO:0000313|Proteomes:UP000004931};
RX PubMed=20601481; DOI=10.1128/JB.00683-10;
RA Oh H.M., Kang I., Ferriera S., Giovannoni S.J., Cho J.C.;
RT "Genome sequence of the oligotrophic marine Gammaproteobacterium HTCC2143,
RT isolated from the Oregon Coast.";
RL J. Bacteriol. 192:4530-4531(2010).
CC -!- FUNCTION: Involved in the transmission of sensory signals from the
CC chemoreceptors to the flagellar motors. CheA is autophosphorylated; it
CC can transfer its phosphate group to either CheB or CheY.
CC {ECO:0000256|ARBA:ARBA00035100}.
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:EAW32858.1}.
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DR EMBL; AAVT01000001; EAW32858.1; -; Genomic_DNA.
DR STRING; 247633.GP2143_16421; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000004931; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR CDD; cd00088; HPT; 3.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 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; 3.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR004105; CheA-like_dim.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
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; 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 PANTHER; PTHR43395:SF8; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 3.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 1.
DR SMART; SM01231; H-kinase_dim; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00073; HPT; 3.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 5.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:EAW32858.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000004931};
KW Transferase {ECO:0000313|EMBL:EAW32858.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 565..669
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 745..849
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1179..1283
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1500..1744
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1746..1885
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 1906..2024
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1093..1126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1451..1478
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 612
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 792
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1226
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1957
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2031 AA; 223621 MW; C30A181E94DDA201 CRC64;
MSERQDFIAL DWVTGEIDET LKQASLSLEA FIINRDDDSN LRFFLSHIHQ VHRTLQMVEF
PDAALLAEEM EALADGLIQQ NIHSSHIEDA LVVLQNAITQ CPLYLEQVKL SRHRLPAMLI
PVLNDLRAAR GEHLLSETVL FAPDLSGLNQ TIDNDQLSIP DSELIEIAQK LRQMFQVALL
GVIRGNDVKN NLNYLAKVCA RLVKLSKGFP PQALWKICIA VLEGLLNGSI EISVAIKMLL
RQVDRQVKSL VESGALGMRQ APPEDLVRNL LYYVARSQST SRFISEAKSE FSLASSLIVE
GEFSNKKMTA ADNIAKDLVT HALIRELVSV RDVLDVSNLL FTMPSIMVRL KAIDDAMAML
GMVASLKKLK KIHHCLTVAS ENAYSIDDEW LDDVKNKIVD LEANLRPADI PELNNSRELF
NDSEEAQQQL DKAFSSVIRE SRQGLEHVRE AIIKFVATQG DQQCLKQMPE LLANIAGSLR
MIPLARAPDL LLSCGRYITG RLLTESSFAD WQQLDKLADA ITSVDYYLER LDSLGDAEER
NILEVAVTSV AELGYPIISD EKRLADEIDP EILEIFVEEV AEVLAEIDQC LLQWNDNYSN
QELGNVVRRA FHTLKGSGRM VGASDVGDLA WSIENMLNRV LEGSITMDAP RLNLIVEARH
EIPTWVDAYE HGTDLDKSLL LSIIHRASAF SDEQDPLLEP EDVIAPTLAD GAGTDAVAIA
EQLIEEASGE AEQKSADNVM ASLFSETMDG ELLEIFATEA AAHGQVLDDF ISHCRDLAGP
AELTDELQRA LHTLKGSANM AGITPVVTIV TPLEHTVKEL RASQLKVDEE LLALLERGSL
YLKAGIEQLA SSPLQPFSDA DHYTAQLKSL LEYRIAKIID TEAEEKGIPP EALNNFLTTS
LDLIIEISGK LVLWQQGDYD LSELGHFQQS MNDFVKHAAS VNMSGPVEFG KVLQIFYRRG
AAQENGHPSD DFFRLAENGN DCLIDMLDQI AGQQTPTFNR PLLSDIENFQ FLTVESAAND
GTDEKVISPP AEANETESED HAVVADDDFD ALLGEFDGDT LIAVLSEDAE LMANSAIVDD
DFADVIGRTV IAGDSSESDQ PGKSDAAIAK SAGEDAESAA TSVDTDEQTF HDLPEVLNSK
QITPVMAELV EEPVTAGNGK FGNVSSAGNR QSVFTQDSDD DIDREILEIF LEEADELLEN
IDETIHSWSV ERDKREYFDD MLRILHTLKG GARLAGLTSL GDLSHNFETS LAHLEGKNGE
IDENTLVSCQ RYQDQLIEQI AAIKSGTGID EGQQNIDGAF IPIDADSVEE FASEATIEGP
LAVDITVDEL KPSSQTSDEL DREVSRELSD LIPDARVEES AVCELESDNT KQGFPEAESA
PDKIAVLKDV DPIKVSFPRS VAPLEAVSLA VDPAIKKAPQ EMVKVSAQLL EELVNLAGET
SISRGRAEEQ ISELVASLDD MQITVDRLQE QVRRLDMETE QQILYRQEQV EIEGSEGFDP
LEMDRYSQLQ QLSRSLLESS SDLVDIKSTL AEKSRDMETL LIQQSRINTD LQEGLMRSRM
VPFSKMVPRL RRIIRQVSGE LGKKVDFHLS NIEGELDRTV LDRMVSPLEH MLRNAVDHGI
ESTDERDAAG KPRRGSVTLD LLREGGEIVF SLSDDGAGVN FDAVKKKAID RGLMMPNSNL
ADHEIAQFIL QPGFSTAEEV TQISGRGVGM DVVNSEIKQL GGSMDIQSVA GKGSRFTVRL
PFTVSVNRAL MVSVSGDSYA IPLNTIEGIV RVSPFELEAY YQPDAPLFEY AGQPYTLRYM
GGLLNRGETP SLEGHSTPLP VVLVRGGEHA IAVQVDSLMG SREIVVKPLG PQFSAVQGLS
GATVLGDGNV VVILDLLALI RADASTIYDD LQLPKIKVPD DDDGLVVMVV DDSVTVRKVT
SRLLERHGMD VLLAKDGVDA VMQLQDLDRI PDVMLLDIEM PRMDGFEVAS RIRHNSRLQD
IPIIMITSRT GEKHRDRALA LGVNEYLGKP YQETELLNII QALTATTSGQ L
//
