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Database: UniProt
Entry: A0A068QW65_9GAMM
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ID   A0A068QW65_9GAMM        Unreviewed;       779 AA.
AC   A0A068QW65;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 60.
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:CDG19193.1};
GN   ORFNames=XDD1_3503 {ECO:0000313|EMBL:CDG19193.1};
OS   Xenorhabdus doucetiae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=351671 {ECO:0000313|EMBL:CDG19193.1, ECO:0000313|Proteomes:UP000032721};
RN   [1] {ECO:0000313|EMBL:CDG19193.1, ECO:0000313|Proteomes:UP000032721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FRM16 / DSM 17909 {ECO:0000313|Proteomes:UP000032721};
RA   Genoscope - CEA;
RL   Submitted (JUL-2013) 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}.
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; FO704550; CDG19193.1; -; Genomic_DNA.
DR   RefSeq; WP_045972771.1; NZ_VNHN01000018.1.
DR   AlphaFoldDB; A0A068QW65; -.
DR   STRING; 351671.XDD1_3503; -.
DR   KEGG; xdo:XDD1_3503; -.
DR   HOGENOM; CLU_000445_114_15_6; -.
DR   OrthoDB; 9770795at2; -.
DR   Proteomes; UP000032721; 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; PTHR43719:SF27; AEROBIC RESPIRATION CONTROL SENSOR PROTEIN ARCB; 1.
DR   PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE 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   Transcription {ECO:0000256|PIRNR:PIRNR003182};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR003182};
KW   Transferase {ECO:0000256|PIRNR:PIRNR003182, ECO:0000313|EMBL:CDG19193.1};
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          679..772
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         718
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003182-50,
FT                   ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   779 AA;  88140 MW;  95B4F669858ABCFE CRC64;
     MKLIRGLAQY YVDLMMKLGL VRFSLLLASA LVILAMAMQM AVTFVLHGEV QLIDLIRSIF
     FGLLITPWAV YFLSIVVEQL EESRQRLSSL VAKLEEMRQR DATLNQQLKE NIAQLNQEIS
     DREKAEKAHL VLLDKLKLEM EHREKTQIEL EQQSVLLRSF LDASPDLVYY RNEDNEFSGC
     NRAMELLTGK SEKQLIGLTP TDVYDKEIAS KVMETDEKVF RHNVSLTYEQ WLVYPDGRKA
     CFELRKVPFY DRVGKRHGLM GFGRDITERK RYQDALENAS RDKTTFISTI SHELRTPLNG
     IVGLSRILLD TDLTPEQSKY LETIHVSAIT LGNIFNDIIE LDKIERRKIQ LDNQPIDFTG
     FMTDLENISG LLAQPKGIKF VLEPEQPLPA KVLTDGTRLR QILWNLISNA VKFTPKGEIK
     VRIWREEGER LLFEVTDSGI GIPADELEKI FAMYYQVKDS AGGRPATGTG IGLAVSKRLA
     QSMGGDIVVK STLGKGSCFT LSVIAPAIDE QPEGKVEQET MPLPALNILL VEDIELNVIV
     ARSVLEKLGN SVDVAMNGHD ALAMFDPDEY DLVLLDIQLP DMTGLDIARQ LHQRYASQSL
     PPLIALTANV LKDKKEYLDA GMDGVLNKPL SVKELTTVIE KYWGKGAESE NILPEVDMMN
     RDEERLDTEM LNQYIELVGA KMIADNLAIF ETMMPGYLAL LDSNMTARDQ KGITEEAHKI
     KGAAGSVGLR HLQQLAQQIQ SPDLPAWWDN VQEWVDELKL EWKQDIEILR NWLPSVTKK
//
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