ID A0A1H3MSL1_9PROT Unreviewed; 723 AA.
AC A0A1H3MSL1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05421754_102232 {ECO:0000313|EMBL:SDY79454.1};
OS Nitrosomonas sp. Nm58.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=200126 {ECO:0000313|EMBL:SDY79454.1, ECO:0000313|Proteomes:UP000199646};
RN [1] {ECO:0000313|Proteomes:UP000199646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nm58 {ECO:0000313|Proteomes:UP000199646};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FNPQ01000022; SDY79454.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3MSL1; -.
DR STRING; 200126.SAMN05421754_102232; -.
DR Proteomes; UP000199646; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR003660; HAMP_dom.
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; IPR017232; NtrY.
DR InterPro; IPR045671; NtrY-like_N.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF19312; NtrY_N; 1.
DR Pfam; PF12860; PAS_7; 1.
DR PIRSF; PIRSF037532; STHK_NtrY; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SDY79454.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000199646};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 34..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 71..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 273..296
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 298..350
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 492..711
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 723 AA; 80736 MW; 01F29B7C78D94250 CRC64;
MKYVITIVTG LSVVMLFLLA TAGANTEFLE RLYRWLIVFN VVFVLFLLVV VGFLLWRLSR
RLKARVFGSR LALRLLTVFS LMAILPGVLV YGISVQFLGK SIESWFDVKV DQALEGGLNL
GQTMLDNLLE ELGKKAKTTA LTLSESPVSP LSALNQLLVQ SQIQEATLFN QEGKAIAFSS
IDDIALFPEI PNAAAMRQIR MQKSYSAVES IPGKGMYLRV LVPVNVLNLD DDIRVLQVLQ
QVPRLLAENA EIVQIGYRNY QELTLSRQGL TRLYGVTLTL ALFLALFSAL AAAFLISEKL
SAPLGMLAEG TRAVAQGDFS RRHRVQSNDE LGILTESFNL MTEQLEVARV TAQRNQQEIE
NARAYLESIL ANLSSGVMVF DEKLHMSTVN RSAEQILQIP LTNLVGLTIE ECAEKESKLR
MLATEIRRGF NSAEMGDWQR QVLHFSESKD QILLLRGSRL PQVTGGGVVV FDDITSLLQV
QRTVAWGEVA RRLAHEIKNP LTPIRLSAER MQHKLMEKLT GQDARILQRS TETIVNQVEA
LKKMVNEFSE YARVPELELY QLDFNRLIHE VLALYETAHT QSDRNHSSKI ILELTADPSL
IRGDPTRLRQ VIHNLLQNAQ DALVDIVDPT ITVRTEILPN GIQFSVSDNG KGFAEQIKAQ
VFEPYVTTKA KGTGLGLPIV KKIIDEHNGT IQIENTQPHG AKVTIVLPRL LSDHTISIPH
QVT
//
