ID A0A143DCM7_9PROT Unreviewed; 992 AA.
AC A0A143DCM7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, 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=AY555_01260 {ECO:0000313|EMBL:AMW34023.1};
OS Haematospirillum jordaniae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Novispirillaceae; Haematospirillum.
OX NCBI_TaxID=1549855 {ECO:0000313|EMBL:AMW34023.1, ECO:0000313|Proteomes:UP000076066};
RN [1] {ECO:0000313|EMBL:AMW34023.1, ECO:0000313|Proteomes:UP000076066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H5569 {ECO:0000313|EMBL:AMW34023.1,
RC ECO:0000313|Proteomes:UP000076066};
RA Nicholson A.C., Humrighouse B.W., Loparov V., McQuiston J.R.;
RT "Complete Genome of H5569, the type strain of the newly described species
RT Haematospirillium jordaniae.";
RL Submitted (FEB-2016) 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; CP014525; AMW34023.1; -; Genomic_DNA.
DR RefSeq; WP_066132361.1; NZ_JAAVTB010000003.1.
DR AlphaFoldDB; A0A143DCM7; -.
DR STRING; 1549855.AY555_01260; -.
DR KEGG; hjo:AY555_01260; -.
DR Proteomes; UP000076066; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR InterPro; IPR007892; CHASE4.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF05228; CHASE4; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF13426; PAS_9; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000076066};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 311..330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 619..691
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 761..982
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 357..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 992 AA; 109638 MW; F2D5D5D2D6FC5062 CRC64;
MSAENPGKWS PLFVDSFTGL STLYQSALDQ AARRYPMTDP YASLPAVVDL PRRHGILNVA
WGGFLAVLSA LVGWLIWLAH EGVDQAKTST DLYARNHIDT EITELRRGQE RLIRDYSLWS
DAWEKLFLLP DPEWIRDNFG QELNSTWGVS RVFIVYGSGP ISEIKQGIPE LMFTEDDPLL
HSVWETASAV REASALSGTH RQASQFFSST GTAWILAAGI LSNPEPLPRD ARLEAMPVLV
MARALDSRWI DGIVRKIGLS SLSIIPASMG HETLDDKDTS MVPLYGTPGQ SVAWLRFTTN
QSPLFYLARR ISLISFGLLL AIALGLILHL RTTVLTRSAL RLNTRLIEEL GSRQYQEHTP
LDKEAAYEEE DTLTEDSRNG HTTTTDVPES SHGIANGYVL IGYSGNIRGA DSGACSLFGY
KNGELDGVPV STLLLTDNGT FSVSMESGAT EQGPRTRRAK ALHKSGTVLP VDLTISHPDD
DHDSLHILIS PRSADKDLAE KFLFMINLLP AGILVHRNLK PLFANQAFMD MVGLDSMEDL
PTPGIQADTL MPMGQNHQDD DDGKTLTTSF ETLYRQNDGS TLRVRTTSFP VLWDGDTAIC
TLMIDITGEH ALRSLQEKTL FRLQQIIDTT EEGYIRLDTD DLIVETNNKT RSILGYQPDD
MQGRPITLFM TQESRNSLNG DVLLEKAETH RRHTLEFVSH DGDVIPLDVS ASILTENDGT
RSGSFVFFRD IRQTLAYEQA LIDARETADR ANRAKSDFLS RMSHELRTPL NAIIGFSQLM
ESSKSETLSD RQRSWLSHIH QSGKLLLTLI DEILDLARIE SGQLTLDIGR VEPSRVIKEC
MGLTDTIARE FGVQVIAAPE TEKAPVVLAD ALRMRQILLN LVSNAIKYNK AGGSVTIGYS
EESPDGYVRI TVTDTGTGLP EERRADIFQP FNRLGQESGP IQGTGIGLSI TGLLVKKMGG
TIDFTSTVGT GSTFWFDLPA AEATKKEITK EV
//
