ID A0A3N9TG73_9VIBR Unreviewed; 790 AA.
AC A0A3N9TG73;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
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:RQW62990.1};
GN ORFNames=EES38_11785 {ECO:0000313|EMBL:RQW62990.1};
OS Vibrio viridaestus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=2487322 {ECO:0000313|EMBL:RQW62990.1, ECO:0000313|Proteomes:UP000281112};
RN [1] {ECO:0000313|EMBL:RQW62990.1, ECO:0000313|Proteomes:UP000281112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LJC006 {ECO:0000313|EMBL:RQW62990.1,
RC ECO:0000313|Proteomes:UP000281112};
RA Liang J.;
RT "Vibrio LJC006 sp. nov., isolated from seawater during the bloom of the
RT enteromorpha.";
RL Submitted (NOV-2018) 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 -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429, ECO:0000256|PIRNR:PIRNR003182}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004429,
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:RQW62990.1}.
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DR EMBL; RJVQ01000004; RQW62990.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N9TG73; -.
DR OrthoDB; 9770795at2; -.
DR Proteomes; UP000281112; 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:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
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|ARBA:ARBA00022840, 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 Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW Kinase {ECO:0000256|PIRNR:PIRNR003182, ECO:0000313|EMBL:RQW62990.1};
KW Membrane {ECO:0000256|PIRNR:PIRNR003182, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR003182};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553,
KW ECO:0000256|PIRSR:PIRSR003182-50};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000281112};
KW Transcription {ECO:0000256|PIRNR:PIRNR003182};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR003182};
KW Transferase {ECO:0000256|PIRNR:PIRNR003182};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW 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..510
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 528..645
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 693..786
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 77..136
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 577
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PIRSR:PIRSR003182-50,
FT ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 732
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PIRSR:PIRSR003182-50,
FT ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 790 AA; 89197 MW; A33C8CA2A48FC248 CRC64;
MKPMKNLAQY YVDLLVKLGI LRFSILLALA LVALAVVVQV GITLALKGFV DDIDIIRSVF
FGLIITPWAV YFLSVVVDQL EESRQRLSKL VSKLKDMRFR DQELNYQLQQ NIVKLNQEIE
ERIKAEEARE EAMVDLENEV YQREKTQLEL AERTALLRSF IDASPDLIYY RNANGVFSGC
NRAMEELTGK RESELVGLSP RQVYSEDVAH LVIETDDHVF KNNCSITYEQ WLEYPDGRKS
YFEIRKVPFY SNEGRHLGLV GFGRDITERK RHEESLEKAS RDKTTFISTI SHELRTPLNG
IVGLSRMLLD TTLTEDQRKY MQTINVSAVT LGNIFNDIID MDKFDRKKLE LFPEPLNFEE
FIVEIESLAA LMAEQKGLRF DLDRLSDLPV AIEIDGTRLR QVIWNLLSNA MKFTKEGGVV
MTVSADIQGA DAFVSIDIED TGIGIPEEDL DKIFAMYYQV KSDKDNLHAV GTGIGLAVSK
QLMNMMNGDI VVSSEEGYGS TFTVTLTAPL AVIPESVTEQ PIQQRSLNIF MVEDIELNVT
VARSLLESLG HTVSVAMTGH EALDMFEPNK FDLVFLDIQL PDMTGFDIAQ TIRQRFQQDG
PLPPLVALTA NVLKDKNEYI RNGMDDAISK PLSVTAVRDV LERQTQISGI EKKVQESSTA
TAGIDMNSTS TDKNDYQSVL DLDMLNSYVD IVGPQPVLDS IKMFEDMMPG YIAILDSNMM
AKDQDAIVSE AHKIKGAAGS IGLARIQKVA QKAQTPEAPA WWENISDWVE EIKNEYSKDI
QLLKQWLENR
//
