ID A0A1N7ITH8_9PROT Unreviewed; 909 AA.
AC A0A1N7ITH8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05421779_101599 {ECO:0000313|EMBL:SIS40409.1};
OS Insolitispirillum peregrinum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Novispirillaceae; Insolitispirillum.
OX NCBI_TaxID=80876 {ECO:0000313|EMBL:SIS40409.1, ECO:0000313|Proteomes:UP000185678};
RN [1] {ECO:0000313|EMBL:SIS40409.1, ECO:0000313|Proteomes:UP000185678}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11589 {ECO:0000313|EMBL:SIS40409.1,
RC ECO:0000313|Proteomes:UP000185678};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FTOA01000001; SIS40409.1; -; Genomic_DNA.
DR RefSeq; WP_076398672.1; NZ_FTOA01000001.1.
DR AlphaFoldDB; A0A1N7ITH8; -.
DR STRING; 80876.SAMN05421779_101599; -.
DR OrthoDB; 7346568at2; -.
DR Proteomes; UP000185678; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 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 InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; 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; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
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; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SIS40409.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000185678};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 260..483
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 647..764
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 808..896
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 696
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 847
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 909 AA; 98039 MW; 3E914513AA21BE8F CRC64;
MNERPAPTSA PPTDDPTALL AALSEQQQRA DYFQRQAEQL AARLVKADAV GSTLRHELEQ
KRRGFSLLAG LSAALTPTSN AHAIFQTTCQ RVNATLNMER TVVLRPVARD TFTVALTQGY
ERNQAEALLA TEIHVPVDTL LQNGYVLITR ESGRDHLHDL RTALSLPFLI AVPVIQDNDV
MAIIITGRTR EQKPFMPRLG QGDRETLQAI AAYVSAIFAQ GAMLDVEHMN QRLRLENERI
SMAKEQAEGL AKAKSEFIAV ISHEVRTPMN GVLGLSRLLL DSDLQPEQQD LAQTIVSSGE
TLLGILNEIL DLSKLEAGRI ELEKLPFHPV SMVEDCMALI AAQASDKGLA LACHAAADVP
DTLIGDGARV RQILMNLIGN AVKFTERGSV SVATSIAPPL PGDAGVTVLF SITDTGIGLS
EEEKTRLFRR YEQAGAWVNR RFGGTGLGLS ISKQLAELMD GTITVHSTLD QGTTFIVTLR
LGHSSSTGPG RPIPHIPEGQ MVLIADPDPI ARQLLTRQLE MWGLIVGQAA TMEDLYDCGP
LLQQGGAIIA STRLGADIAA CLQTVASNSG VGSSPRALIL SCGSKRLPPA KETAIPWIAE
PIRESSLKAA IEWLFAAPSK RSNTPSPHFA VMSPPVEGPS PSLPSLSILL AEDNIVNQRV
AIGLLERQGA RVVAVENGRQ ALAALQHTRF DLILMDRHMP DMNGIEAVQA LRRLPPPYGT
LPVIALTAAA SQADAQECLD AGMNAFVSKP IDPKQLYQVI LSLVEPSSSA QTPALRLPAP
TLLPTRGICA GHNPNDPAII ADLVRDLGID ILQELNNDFS HSCRNLLDTI NTAISTRNHS
EMEYATHSLK SAAGFLGIRE LADAAAEIEQ QAKMQAETVW QAAARLSMLA ADGQRWLAAM
TLHHTQNHR
//
