ID A0A014NNN1_9GAMM Unreviewed; 778 AA.
AC A0A014NNN1;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Aerobic respiration control sensor protein {ECO:0000256|PIRNR:PIRNR003182};
DE EC=2.7.13.3 {ECO:0000256|PIRNR:PIRNR003182};
GN ORFNames=BG55_09545 {ECO:0000313|EMBL:EXU75425.1};
OS Erwinia mallotivora.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=69222 {ECO:0000313|EMBL:EXU75425.1, ECO:0000313|Proteomes:UP000019918};
RN [1] {ECO:0000313|EMBL:EXU75425.1, ECO:0000313|Proteomes:UP000019918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BT-MARDI {ECO:0000313|EMBL:EXU75425.1,
RC ECO:0000313|Proteomes:UP000019918};
RA Redzuan R., Abu Bakar N., Badrun R., Mohd Raih M.F., Rozano L.,
RA Mat Amin N.;
RT "Draft genome of Erwinia mallotivora strain BT-MARDI, a papaya dieback
RT pathogen.";
RL Submitted (FEB-2014) 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 ECO:0000256|PIRNR:PIRNR003182};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|PIRNR:PIRNR003182}; Multi-pass membrane protein
CC {ECO:0000256|PIRNR:PIRNR003182}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXU75425.1}.
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DR EMBL; JFHN01000045; EXU75425.1; -; Genomic_DNA.
DR RefSeq; WP_034936710.1; NZ_JFHN01000045.1.
DR AlphaFoldDB; A0A014NNN1; -.
DR STRING; 69222.BG55_09545; -.
DR PATRIC; fig|69222.5.peg.1966; -.
DR OrthoDB; 9770795at2; -.
DR Proteomes; UP000019918; Unassembled WGS sequence.
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:SF79; HISTIDINE KINASE; 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:UP000019918};
KW Transcription {ECO:0000256|PIRNR:PIRNR003182};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR003182};
KW Transferase {ECO:0000256|PIRNR:PIRNR003182};
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 678..771
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 717
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PIRSR:PIRSR003182-50,
FT ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 778 AA; 88367 MW; 795B96F7B91E3B8E CRC64;
MKQIRLLAQY YVDLMVKLGL VRFSLLLASA LVVLAMIVQM AVTMVLRGHV ESIDMVRSVF
FGLLITPWAV YFLSVVVEQL EESRQRLSRL VDKLEEMRHR DLELNQQMKG NITQLNQEIA
DRIRAEKARL QVLDKLTEEM ERREQAQIEL EQQSSFLRSF LDASPDLVFY RNIDQQFSGC
NRAMELLTGK SEKQLIGLTP RDVYDQEGAN KVLETDEKVF RHNVSLTYEQ WLQYPDGRKA
CFEIRKVPYY DRVGKRSGLM GFGRDITERK RYQDALENAS REKTTFISTI SHELRTPLNG
IVGLSRILLD TDLNAEQLKY LKTIHVSAIT LGNIFNDVIE MDKIERRKVQ LDNQPVDFTG
FLADLENLSG LLVQPKGLTF MLQPELPLPN TVVTDGTRLR QILWNLIGNA VKFTQQGSVV
VRVCYQPDGC LRFDVEDSGM GIPQYEQDKI FAMYYQVKDQ RGGKPATGTG IGLAVSKRLA
QGMGGDITVR SAPGAGSCFT LTVMAPRLAQ QDEEQQPIDE LPLPALHVLL VEDIELNVVV
ARSVLEKLGN SVEVAMTGEE ALTLFDPAEF DLVLLDIQLP NMSGLEVARE IHQRYAGQQL
PPLIALTANV LKDKKEYLEA GMDDVLSKPL AVPALTAIIQ KYWDYQQGDE QTQEYQLDEK
KSQLLDITML EDYIELVGPE LIHQSLTIFE QMMPGYLAVL DSNMMARDQK GITEEGHKIK
GAAGSVGLVH LQQLAKQIQS PELPAWWDNV QEWIEELKQD WRHDVEVLRE WVTASQKK
//
