ID A0A1G8FLJ1_9RHOO Unreviewed; 1154 AA.
AC A0A1G8FLJ1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05660652_02356 {ECO:0000313|EMBL:SDH82876.1};
OS Propionivibrio dicarboxylicus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Propionivibrio.
OX NCBI_TaxID=83767 {ECO:0000313|EMBL:SDH82876.1, ECO:0000313|Proteomes:UP000198607};
RN [1] {ECO:0000313|EMBL:SDH82876.1, ECO:0000313|Proteomes:UP000198607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5885 {ECO:0000313|EMBL:SDH82876.1,
RC ECO:0000313|Proteomes:UP000198607};
RA de Groot N.N.;
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; FNCY01000009; SDH82876.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8FLJ1; -.
DR STRING; 83767.SAMN05660652_02356; -.
DR Proteomes; UP000198607; 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 CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd12914; PDC1_DGC_like; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 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; 4.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR033479; dCache_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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR029151; Sensor-like_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13426; PAS_9; 2.
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; 3.
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); 3.
DR SUPFAM; SSF103190; Sensory domain-like; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
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:UP000198607};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 289..308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 309..362
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 367..436
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 441..491
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 569..622
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 623..670
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 697..747
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 783..1003
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1031..1147
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 735..769
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1080
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1154 AA; 127949 MW; 79D5A29113ED3BD8 CRC64;
MFGQPISLKV RITVAMLSVM VLALWVLSWF GSRSLRLDME SVLGNQQFAT ASYIAAEIEN
NVSARVAALE LIAAAIPPKL FEKTPALQDF LDQRFVLHQQ FNGGVMITGH DGVVIASTPK
SLERIGHDFS DRDHIAAALR GRKAIGSPVV GRALKAPLIG ISVPIRDRTG RVIGVLAGVT
DLSRPNFLQH VAESRYGRTG GYLLVDRKNR LIVTASEKDR TMQSASPPGA NPTVDRFIAG
YEGALVYTNQ KDVEILASVK QIAGTDWYFA VSLPTQEAFG PIREMQERML WATLLLTLLG
GVAAWLLLRQ SLNPMMSTAA LLADMSEDKT PLKRLPILQD DEIGHLVAGF NRLLDSLSAK
DVALRRSEAR YRASVQASQD FINITRMSDG CYVEVNQAFL DSTGYRRDEV IGRTSIDLGI
WADPEDRDRL VNALRRDGKC LNLEARYRRK NGELGWGVMS ASLVQIDGEA MVVSVTRETT
EWKRADERLR ENEMRFRTIS ELTSDLTYSC RREADGPFVI DWMIGNAEQV LGYSIEAMLS
MGCWKPLVLN EDVPVFDSAI AALQPGQSSR VTLRLKVRDG SVRYFDSVAR AELADPLGGG
HRLYGSLCDV TERRRAEIAL TESEAHYRVM YEASQDLIAV VRLDDGVFIE ANDVYLSVLG
YARDEVVGHS SEDLHIWADT EQRDAFVARL CQEQRCWNHE ACLNTRDGRQ VWGLVSASII
ETRGHACIFS VTRDITKLKE TEQELRHYRQ RLENLVDERT RALVEANRAA ESASMAKSMF
LANMSHEIRT PMNAIVGITN ILRRTPLTAE QAERLGQIDT ATQHLLKVIN DILDLSKIEA
GKLMLEEQHL SVEVLLADVV ALVADRVNAK HLVLNVEADT FPDCLYGDAT RIRQALLNYV
SNAIKFTEHG TIDLRATKML DQCDAVVVRF EVRDSGVGIR EEDLSRIFSA FEQADGTTTR
RHGGTGLGLA ITRRLALMMG GEVGVESRFG EGSLFWFSVC LRKASSPSAI EVALAGEAAE
QTIREHYAGK RVLLVDDEPV NLEVARSFLE GGGLLVDVAS DGHQAVAMAS SSTYALILMD
MLMPGLDGLD ATRQIRWYPQ CRGIPIVAMT ANAFVEDRKR CIEAGMNDFL SKPFAPETLF
SVVLRWLSSP PESV
//
