ID D8MXL9_ERWBE Unreviewed; 776 AA.
AC D8MXL9;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=Aerobic respiration control sensor protein {ECO:0000256|PIRNR:PIRNR003182};
DE EC=2.7.13.3 {ECO:0000256|PIRNR:PIRNR003182};
GN Name=arcB {ECO:0000313|EMBL:CAX61576.1};
GN OrderedLocusNames=EbC_40450 {ECO:0000313|EMBL:CAX61576.1};
OS Erwinia billingiae (strain Eb661).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=634500 {ECO:0000313|Proteomes:UP000008793};
RN [1] {ECO:0000313|EMBL:CAX61576.1, ECO:0000313|Proteomes:UP000008793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eb661 {ECO:0000313|EMBL:CAX61576.1,
RC ECO:0000313|Proteomes:UP000008793};
RX PubMed=20565991; DOI=10.1186/1471-2164-11-393;
RA Kube M., Migdoll A.M., Gehring I., Heitmann K., Mayer Y., Kuhl H.,
RA Knaust F., Geider K., Reinhardt R.;
RT "Genome comparison of the epiphytic bacteria Erwinia billingiae and E.
RT tasmaniensis with the pear pathogen E. pyrifoliae.";
RL BMC Genomics 11:393-393(2010).
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 ECO:0000256|PIRNR:PIRNR003182};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|PIRNR:PIRNR003182}; Multi-pass membrane protein
CC {ECO:0000256|PIRNR:PIRNR003182}.
CC -!- PTM: Activation requires a sequential transfer of a phosphate group
CC from a His in the primary transmitter domain, to an Asp in the receiver
CC domain and to a His in the secondary transmitter domain.
CC {ECO:0000256|PIRSR:PIRSR003182-50}.
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DR EMBL; FP236843; CAX61576.1; -; Genomic_DNA.
DR RefSeq; WP_013204059.1; NC_014306.1.
DR AlphaFoldDB; D8MXL9; -.
DR STRING; 634500.EbC_40450; -.
DR KEGG; ebi:EbC_40450; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_114_15_6; -.
DR Proteomes; UP000008793; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd00130; PAS; 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; 1.10.287.970; His Kinase A (phosphoacceptor) domain; 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 Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR027460; ArcB_TM_sf.
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; IPR040642; HKR_ArcB_TM.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR014409; Sig_transdc_His_kin_hyb_ArcB.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF18415; HKR_ArcB_TM; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PIRSF; PIRSF003182; ArcB; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00091; PAS; 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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 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; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR003182};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519,
KW ECO:0000256|PIRNR:PIRNR003182};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|PIRNR:PIRNR003182}; Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|PIRNR:PIRNR003182};
KW Membrane {ECO:0000256|PIRNR:PIRNR003182, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR003182};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553,
KW ECO:0000256|PIRSR:PIRSR003182-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000008793};
KW Transcription {ECO:0000256|PIRNR:PIRNR003182};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR003182};
KW Transferase {ECO:0000256|PIRNR:PIRNR003182, ECO:0000313|EMBL:CAX61576.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012,
KW ECO:0000256|PIRNR:PIRNR003182}.
FT TRANSMEM 20..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 58..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 153..223
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 226..278
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 289..507
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 527..643
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 676..769
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 77..153
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 292
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR003182-50"
FT MOD_RES 576
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PIRSR:PIRSR003182-50,
FT ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 715
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PIRSR:PIRSR003182-50,
FT ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 776 AA; 88244 MW; F4C23B62C420BF3C CRC64;
MKQIRLLAQY YVDLMVKLGL VRFSLLLASA LVVLAMIVQM AVTMVLRGHV ESIDMVRSVF
FGLLITPWAV YFLSVVVEQL EESRQRLSRL VDKLEEMRHR DLELNQQMKE NITQLNHEIA
DRIKAEEARL QVMAKLKEEM ARREEAQIEL EQQSSFLRSF LDASPDLVFY RNIDQQFSGC
NRAMELLTGK SEKQLIGLTP RDVYDEDAAT KVLETDDKVF RHNVSLTYEQ WLQYPDGRKA
CFEIRKVPYY DRIGKRSGLM GFGRDITERK RYQDALENAS REKTTFISTI SHELRTPLNG
IVGLSRILLD TDLNQEQLKY LKTIHVSAIT LGNIFNDVIE MDKIERRKVQ LDIQPVDFTG
FLADLENLSG LLAQPKELKF VLDPQLPLPH KIMTDGTRLR QILWNLIGNA VKFTQKGSII
VRVAYLGEDC LRFEVEDSGM GIPQDEQDKI FAMYYQVKDQ HGGKPATGTG IGLAVSRRLA
QSMGGDITVH SAPGTGSCFT LTVNAPRIAE QPEDQQPADD MPLPALHVLL VEDIELNVVV
ARSVLEKLGN SVEVAMTGEE ALAMFDPEEF DLVLLDIQLP DMTGLDVARE IHQRHGKQHL
PPLVALTANV LKDKKEYLDA GMDDVLSKPL AVPALTAIIK KYWDFQQDEA EERKVDEKKL
GLLDVTMLEQ YIELVGPQLI YQSMEMFEQM MPGYLDVLDS NMMARDQKGI AEEGHKIKGA
AGSVGLVHLQ QLAKQIQSPE LPAWWDNVQE WIDELKQEWR NDVDVLREWV SDAGKK
//
