ID I4VZI8_9GAMM Unreviewed; 2017 AA.
AC I4VZI8;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=UU9_01759 {ECO:0000313|EMBL:EIL92629.1};
OS Rhodanobacter fulvus Jip2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1163408 {ECO:0000313|EMBL:EIL92629.1, ECO:0000313|Proteomes:UP000004210};
RN [1] {ECO:0000313|EMBL:EIL92629.1, ECO:0000313|Proteomes:UP000004210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Jip2T {ECO:0000313|Proteomes:UP000004210};
RX PubMed=22843592; DOI=10.1128/JB.00871-12;
RA Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S.,
RA Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N.,
RA Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.;
RT "Genome sequences for six rhodanobacter strains, isolated from soils and
RT the terrestrial subsurface, with variable denitrification capabilities.";
RL J. Bacteriol. 194:4461-4462(2012).
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:EIL92629.1}.
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DR EMBL; AJXU01000007; EIL92629.1; -; Genomic_DNA.
DR RefSeq; WP_007079994.1; NZ_AJXU01000007.1.
DR STRING; 1163408.UU9_01759; -.
DR PATRIC; fig|1163408.3.peg.366; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000004210; 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; 2.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.287.560; Histidine kinase CheA-like, homodimeric domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 4.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR004105; CheA-like_dim.
DR InterPro; IPR037006; CheA-like_homodim_sf.
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};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000004210};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 676..780
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 868..972
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1225..1327
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1493..1726
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1728..1865
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 1891..2007
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1142..1200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1424..1458
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1142..1193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 723
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 912
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1272
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1940
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2017 AA; 218945 MW; DCD6F449841A558F CRC64;
MRLQDHIDFT TLQWVKPQLD EALSSARDAL ATHVENPADR SVMRSCMDQL HQVRGTLQMV
ELHGAAMAAA EMEAVSRALL DDQVGNREEA YAVLMRGLMQ LPDYLERLSG GHRDVPVVLL
PLLNDLRGVI EKPPLSESAL FHPNLDAFLP EQAPAAMSES HAEARRGELT ALRLRFQRQL
LGWFRGEDPT RQLAGMRTTL LEIAARCYHV HGRRLWWIAA GVLEGLGQGL FKNRTTEIRQ
LIGKVDRNIR ELVEHGEDSL RGGDADELAC QLLYLVAQSP QRSPQMELLQ STYALDRQVP
DASELEHARG SMAGHNRALL DSVSRALKDD LLRVKEALDL FLRQVDGDPA QLAAQGEVLE
RVGDTLGMLA LAVPRRMVVE QRQVLDEIAN HMRSADEAAL LDVAGALLYV EASLDDHIES
LGAEGVTEGD EGVVGVPRSE AMGIVVALMQ EAISNTGKVK DAIVAFSESG WQHEHLAGSP
ALMDEVAGAL RMLSTARPAE LAEGISRFIG NELLLDRRVP DGAQMDHLAD ALAALEYYLE
AAREHRGGLE HILDVAEHSL GLLGYWPPPA ARELPETLPP VAVDALSTDD EHVELSESVS
VHPGDSIHEL IIGGDESSPR SAQDIDGLRL AETESLKPES AESAADEDWV EIEEEIVEQV
PVTDPRAATA GFNANAEGID DDIREIFLEE MQEEIDNLTE AEKVWLDDPS QLSSLTAIRR
SFHTLKGSGR LVGASVLGEF AWKVESALNR VLDNSIEPHE GVQAMVRHAI DALPQLLAAL
KGEGTLKAPL GAIMDVAERL AAGEQGARVE GHPSVVTETV RRVVRRRVPR MDADAAAIPQ
AGITDAHTLA GAPDDDIEPV EALPLPVMPP VDPVLLEILR SEVAQYLQTI RGAIHRAGTE
LRVGEELLRA VHTLHGAIAM VDIALLMQVL SPLEGLLKRL RAADVPLSSE GLRLLGEAAD
VVDTVMEQFD AADPQLPVVD TLVDQIVAMR DLYSESQVAH VVYESRPDDL EDAAAALGAE
HDLDAWVPSH ELDATPVDND EAPAIADEAP ADEALSGASP AVTFGDGIEP AADADDAHHE
TFANELMAAL DAFEPGETRD SDIEDDDVVR TDDENAAVDA QQDELDDTGL AEELAAELEA
VEREAAAREA AEREAAAQRE AEARASAERE AAEREAAQRR EREARELAER EASEAAALAR
QATHAVDAGV ASTTVEGGAE EAPAANALDD DLLEVFLDEA HEILDHADGV LAQWRAEPAE
LGYVGELQRD LHTLKGGARI SGLAAIGDLA HAIETLLEKP VESAGTPSLI GALESSFDQL
NAMVQQVAHR QAVEYPQAAI DRLLALAGEE GFTNDDVLAA IAMPEAASPT SPVAASGERT
PDGDLPGLLP EAEEEVRSTQ EQIRVRADLL DSLVNHAGEV AIYRSRLEQQ VAGYRFNLVE
LEQTVARLRS QLRMLEIETE AQIIARFQRE HREAGLTTVF DPLELDRYSQ LQQYSRALAE
SVSDLVSIQS TLDELTRQAE TLLIQQSRVS TDLQDGLLRT RMLPFDTMVP NLRRTLRQAA
QEEGKHAQLY VDGAHGEMDR NLLDRIKAPF EHMLRNAIAH GIETPDERRK VGKPAEGAVH
IRVAREATEV VVRVSDDGRG LDREAIRARG IERGLLRADA NPSDDQLLGL ITQAGFSTAG
KITQLAGRGV GMDVVANEIK QLGGSLSIES TAGKGTTFVL RLPFTLAVTQ AILVRIGEAT
FAIPMTSVQG VARIDAEEMT ALLEQGEPTF SHGNEPYAIH DLAELLGLPP GLPPEGEQQP
LLLTRAGDLR AAIRIDAVLG SHEIVVKSVG PQISSVPGLL GATIMGDGSV LIILDLAPLV
RHGITRREQR LAEGLSALQA PVIEEVRVRP LVMVVDDSIT MRKVTSRVLE RHEYEVSTAK
DGVDAVEKLH ERVPDLMLLD IEMPRMDGYE LATLMKADPR LSGVPIIMIT SRSGDKHRQR
ALDIGVERYL GKPYQEADLL TQIGEVLELH ASEPAHD
//
