ID A0A1M6GFR3_MALRU Unreviewed; 830 AA.
AC A0A1M6GFR3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN02745165_01535 {ECO:0000313|EMBL:SHJ08790.1};
OS Malonomonas rubra DSM 5091.
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Desulfuromonadales;
OC Geopsychrobacteraceae; Malonomonas.
OX NCBI_TaxID=1122189 {ECO:0000313|EMBL:SHJ08790.1, ECO:0000313|Proteomes:UP000184171};
RN [1] {ECO:0000313|EMBL:SHJ08790.1, ECO:0000313|Proteomes:UP000184171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5091 {ECO:0000313|EMBL:SHJ08790.1,
RC ECO:0000313|Proteomes:UP000184171};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FQZT01000004; SHJ08790.1; -; Genomic_DNA.
DR RefSeq; WP_072907493.1; NZ_FQZT01000004.1.
DR AlphaFoldDB; A0A1M6GFR3; -.
DR STRING; 1122189.SAMN02745165_01535; -.
DR OrthoDB; 9806821at2; -.
DR Proteomes; UP000184171; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 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; IPR011006; CheY-like_superfamily.
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; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR011620; Sig_transdc_His_kinase_LytS_TM.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF07694; 5TM-5TMR_LYT; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 2.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000184171};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 68..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 135..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 203..245
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 277..329
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 466..691
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 711..827
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 762
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 830 AA; 92668 MW; E8F38EF317255F4A CRC64;
MNFLIELINN VALLITLGLL YDISSRRETE NQLSPMPLVF GLGIGLISIV LMSTPAKFSP
GIIFDTRTIL LCVTGLYFGP LTTVIAMLVA IAYRYHIGGI GTIAGAATII TSGTIGILWN
RYRYREDKLY SLKELYLFGF TVHAVMLLCM FLLPAEVIQK TLKVLVIPAI FIYPLGTMLL
GYLLGVRKKH FLTEKKLQLV SRREQELADI VRNAPVGIAT GYPDGTLEIC NANFSEMTGY
STAELETVRW NDMLTPGKWR ALEEEELKRL NPQKRIVQYE KEFLCKDGKI LPVEMTVSGG
FDSNGKPTYY FAFAQDITTR KMAERKDKAN QQQLITILNS IDANVYVADL ESYEILFMNN
NMIQDFGQDL TGEICWKVFR GESGPCPACK NDLLVDENGQ PTDGSVWDNQ NPITGKYYIN
HDRAIEWLDG QLVHLQISTD ISHIKSMEEQ LRQKYKMEAI GVMAGGMAHN FNNNLSVILG
NLELAKMKLT GASEIDELLD HAKIAVLRSR DLIKQIMTYS RKEEKDKTAL QLAVTIEEVM
LLLKSTIPSS VYIQQKLSPA SITQTIHANA TQIQEILLNL CNNAVHAMDE QGTLTIGLDT
VELDRRQIPA NSLGQPGSYL HLWVQDTGCG IASDLLDKIF DPFFTTKALH EGTGMGLSTV
QGIMRHLHGV TRVESQIGEG TTVHLYFPVT EQNEGKQVGT IDIEPFKGKE SVLFVDDDEM
IASMAQSALS GMGYQVTTLT DSHEALKLFT DDPGRFDLVI TDQTMPEMTG RDLILQLKQV
RSDIPTIICT GYSSKVDEAE AEKLGADIFL MKPMELPELL KTVRQVLDKK
//
