ID A0A1X9NIA4_9GAMM Unreviewed; 2142 AA.
AC A0A1X9NIA4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BST96_06055 {ECO:0000313|EMBL:ARN73713.1};
OS Oceanicoccus sagamiensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Spongiibacteraceae; Oceanicoccus.
OX NCBI_TaxID=716816 {ECO:0000313|EMBL:ARN73713.1, ECO:0000313|Proteomes:UP000193450};
RN [1] {ECO:0000313|EMBL:ARN73713.1, ECO:0000313|Proteomes:UP000193450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 107125 {ECO:0000313|EMBL:ARN73713.1,
RC ECO:0000313|Proteomes:UP000193450};
RA Kumagai Y.;
RT "Trade-off between light-utilization and light-protection in marine
RT flavobacteria.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; CP019343; ARN73713.1; -; Genomic_DNA.
DR STRING; 716816.BST96_06055; -.
DR KEGG; osg:BST96_06055; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000193450; Chromosome.
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; 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; 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 Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000193450};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 631..735
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 868..972
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1302..1406
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1613..1857
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1859..1998
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 2019..2137
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1262..1302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1419..1452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1477..1505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1263..1302
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 678
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 915
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1349
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 2070
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2142 AA; 234852 MW; F9092A5D7EB56FBE CRC64;
MSERQDFIAL EWVAGEIGET LNQAAQALEA YIANRDDSTK LRFCLTHIHQ VHGTLQMVEF
FGAALLAEEM EGVAEALTQN KIHGSHIDDA LDVLRHAIAQ LPVYLEKVKE SRHGLPATLL
PVLNDLRAVR GESLLSETVL FAPQMVSAHN HVDGELQVST AELAEIAHKL RQMFQIALLG
FIRGNDIKKN LNYLAKVCAR LVKLTESFPS QPLWKVCIAV LEGLLNGSIE SSVAVKILLR
QVDRQIKNII DEGEAAIKRG APDDLLKNLL YYVARSKANS RYIQEIKTEY QLEQSLLGET
ELDDETLATP DAGVMQSVVE ALVQEMKDIQ LALADAGSDA AALTEVLPLF RRVNDTMAIL
GMGGALKQVQ EPYTRLAKAL ATQDVVADNE LQQISEQLAT AEAELNPNAV INSTDEQALF
NDSEEAQEHL DLAFESVVRE SRNGLEQAKE AIIEFVATQW NHNSLSDLPS LLNEIHGSLN
MVPLTRAAQV IKSCEHYVSE SLLAQKAIPE WQVLDTLADA ITSIDYYLER LSDGNASEGE
AILDVAAESA AELGYPIALS ASADDQVPVL DDVETEPEAP LETLAEETVE QEETAAADIP
VLAEVIPLHG SAAEEPEQPA ADMAAKAVED DEDFDPEIVE IFIEEAGEVL ETIDEFLPQW
QADHNDEEAR STVRRAFHTL KGSGRMVGAT DIGELAWSVE NMLNRVMEGS ITIDQVRFDL
MAETRSTVPE LVTAFEQRQQ VDKAVFEPLI ERANALAAEQ TPELSDVVES ATVAEDIADN
SAEEMAENIS EEIVEPIAEQ DIDQATEDSS EALADNIPVL EETEASATLS EAETLLRMPV
ITDSQAETLL RTPVVTDSDL EAAELNSEEE LDAELIEIFA SEAALHGQVL DDFIAHCKEL
AGPAELTDVL QRALHTLKGS ANMAGVLPVV GVVTPVELVV KELRASQLKV DAPLVELLER
GSLLIKAGIE QLAITPLQDL PGVDDYVEEL MALFNQRIAD AADVEQADNG IPPEALNQFL
TESLDLITEI SGRLVLWQQG DIEPGEPALL ESLMDRFIVH AESVNMLAPV EFGQQVQVLY
RRAAELDPKA IADDFFELSN RANDSLIDML DQIAGHQTPV FDAEIYGEVE DFEFAEIDIA
PAQAAEAITE SADPAFELSD SVDDNDLLDV LAEDSELMEA SEVVELDLDA TVSMAIVDDS
HLPSDEDVEI EDFAIDDSVA TVAFDTVDVD ASEIEEPAVD NETIVAAMSN LADAVADLEQ
EPEAIQPEPE PEPEPEPEPE PEPEPEPVAE AEPVAADAEE DDDEIDDEII EIFLEEADDL
LENLDEAIHG WMDDRGNRSY LDDLLRILHT LKGGARLAGM TPVGNLSHNF ETSLIGLENQ
QTDVSDETLN DIQNYQDQLL AQITAVKAGE AIADVEQMEE PELEQPGAEA VAEDEAEATP
EPEPSVELEE ASDLSFDESF DMDDIDIEAA TGDDLVAQES DADDSPEQAL PERAAEPEPS
TTIVPLEAQR PREVSAVEIA TQLVDPNQKK GPQEVVKVSA SLLEELVNLA GETSISRGRT
EEQVSELVFS LDEMQITVDR LQEQVRRLDM ETEQQILYRQ EQVESEGLEG FDPLEMDRYS
QLQQLSRSLL ESSSDLIDIK STLADKSRDM ETLLIQQSRI NTELQEGLMR SQMVPFSRMV
PRLRRIIRQI SGELNKKVDF QLDNIEGELD RTVLERMVAP LEHMLRNAVD HGIETAEQRK
ESGKAARGNV TLGLAREGGE VVITLSDDGG GINLDAVKSK AIERGLMEAD ADLTDHEILQ
FILQAGFSTA TEVTQISGRG VGMDVVHSEI KQLGGSMDID SKLGQGTSFV VRLPFTVSVN
RALMVRVGTD IYAIPLNSIE GIVRVSPFEL EAYYQPDAPM FEYAGQPYLL RYMGALLHRG
EKPNLEGQSM PLPVVLVRGA EHSVAIQVDN LMGSREIVVK PLGPQFSTVQ GLSGATVLGD
GSVVVILDLL AMIRADASHM YRDFIAGQEE QIDDDRNTIV MVVDDSVTVR KVTSRLLERQ
GMDVVLAKDG VDAVTQLQEI EVIPDVMLLD IEMPRMDGFE VASRVRHNSR LKDIPIIMIT
SRTGEKHRER ALSLGVNEYM GKPYQESVLL ETINTLTGAT AE
//
