ID G4QJX5_GLANF Unreviewed; 735 AA.
AC G4QJX5;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
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:AEP29017.1};
GN OrderedLocusNames=GNIT_0879 {ECO:0000313|EMBL:AEP29017.1};
OS Glaciecola nitratireducens (strain JCM 12485 / KCTC 12276 / FR1064).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Glaciecola.
OX NCBI_TaxID=1085623 {ECO:0000313|EMBL:AEP29017.1, ECO:0000313|Proteomes:UP000009282};
RN [1] {ECO:0000313|EMBL:AEP29017.1, ECO:0000313|Proteomes:UP000009282}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 12485 / KCTC 12276 / FR1064
RC {ECO:0000313|Proteomes:UP000009282};
RX PubMed=22123761; DOI=10.1128/JB.06296-11;
RA Bian F., Qin Q.L., Xie B.B., Shu Y.L., Zhang X.Y., Yu Y., Chen B.,
RA Chen X.L., Zhou B.C., Zhang Y.Z.;
RT "Complete genome sequence of seawater bacterium Glaciecola nitratireducens
RT FR1064T.";
RL J. Bacteriol. 193:7006-7007(2011).
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; CP003060; AEP29017.1; -; Genomic_DNA.
DR AlphaFoldDB; G4QJX5; -.
DR STRING; 1085623.GNIT_0879; -.
DR KEGG; gni:GNIT_0879; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_114_15_6; -.
DR Proteomes; UP000009282; 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 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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
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; PF08448; PAS_4; 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; SM00086; PAC; 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|PIRNR:PIRNR003182};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|PIRNR:PIRNR003182};
KW Membrane {ECO:0000256|PIRNR:PIRNR003182};
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:UP000009282};
KW Transcription {ECO:0000256|PIRNR:PIRNR003182};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR003182};
KW Transferase {ECO:0000256|PIRNR:PIRNR003182};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012,
KW ECO:0000256|PIRNR:PIRNR003182}.
FT DOMAIN 108..152
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 181..233
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 244..465
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 481..596
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 634..727
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 32..108
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 247
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR003182-50"
FT MOD_RES 530
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PIRSR:PIRSR003182-50,
FT ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 673
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PIRSR:PIRSR003182-50,
FT ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 735 AA; 83281 MW; A193FD913B7234C4 CRC64;
MGSPVDPDDF ITALILTLLS APWVLYFFSE LIKQLEHSRI NLEDAVSQLE RLRKHDVILN
RELQNNIRQL NYEIEQRRNA QLERESVFEE LEREIKEKSE QEIQARRLST LTRSIIDASP
DLIYYRNEEG RFAGCNRVAE EVTGKTEAEL LGLTPHQVYD EHLARQVAAS DHEVLETNAS
LTEELWLQFA DGRRRYFEMR KVPFFDQDGH RLGLLAFGRD MTERKQAESA IAQASKDKTK
FVATISHELR TPLNGIVGLS RMLRDTKLSK EQFDWVSTIY ASAITLGNIF NDIVDLDKLD
RDKIEIDLKT VNLRDFTNEI SSIVSLLAQD KSLKFHSEII EPIPVAIEAD GTRLRQVLWN
ILFNAIKFTQ KGEVKLSIEA SDEGAGNAKV TFRITDSGIG IPQDDLDKIF AMYYQVDHPD
HKSATGTGIG LAICKQMVDK MGGEIHVHSV IGQGTCFEIV LPVAISQHQA RMAELEVSNL
NILLVEDIEL NVLVAKALLE KLGQRVEVAM TGTAAIEMAR KTEYDLILLD IQLPDMSGFD
VAKVLHEEEL VLQTPIVALT ANVIKKREEY LQNGMDDIIA KPIKKSRVIE VFNELFGEEQ
KHEERRPTSE LVSIPKVDKI LDVDMLQMLV DTIGEDMVRA SLGIFKEKIP EYMELLTVSL
AANEKAEVCS QAHKIKGAAG SVGLMRVQQT ANKIQEGDHP AWWENVHEWV EELAMAIDKD
VEHLMEWVNA NKIDD
//
