ID K6Y9D8_9ALTE Unreviewed; 781 AA.
AC K6Y9D8;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, 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:GAC20581.1};
GN ORFNames=GARC_3627 {ECO:0000313|EMBL:GAC20581.1};
OS Paraglaciecola arctica BSs20135.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=493475 {ECO:0000313|EMBL:GAC20581.1, ECO:0000313|Proteomes:UP000006327};
RN [1] {ECO:0000313|EMBL:GAC20581.1, ECO:0000313|Proteomes:UP000006327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSs20135 {ECO:0000313|EMBL:GAC20581.1,
RC ECO:0000313|Proteomes:UP000006327};
RX PubMed=25009843;
RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT high degree of genomic diversity and genomic characteristic for cold
RT adaptation.";
RL Environ. Microbiol. 16:1642-1653(2014).
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}.
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:GAC20581.1}.
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DR EMBL; BAEO01000055; GAC20581.1; -; Genomic_DNA.
DR RefSeq; WP_007622637.1; NZ_BAEO01000055.1.
DR AlphaFoldDB; K6Y9D8; -.
DR STRING; 493475.GARC_3627; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR OrthoDB; 9810730at2; -.
DR Proteomes; UP000006327; 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 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; 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; 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; 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; 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, ECO:0000313|EMBL:GAC20581.1};
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:UP000006327};
KW Transcription {ECO:0000256|PIRNR:PIRNR003182};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR003182};
KW Transferase {ECO:0000256|PIRNR:PIRNR003182, ECO:0000313|EMBL:GAC20581.1};
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 21..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 156..226
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 229..281
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 292..513
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 529..644
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 680..773
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 80..133
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 295
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR003182-50"
FT MOD_RES 578
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PIRSR:PIRSR003182-50,
FT ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 719
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PIRSR:PIRSR003182-50,
FT ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 781 AA; 88024 MW; E758F1B3C7208527 CRC64;
MTKKTSVEPW AMRIAQLINR FGAVKSSILF VIVTLIFTFA GTYFLRGIIS DNAHTEDFIS
ASILTLLSAP WVLWFFSELV KQLERSRESL EYAVTQLEKL REEDELLNHT LQNNIKQLNH
EIEQRKNAQL ERESVFTDLE REITEKSEKE KQASQLSTLL RSIIDASPDL IYYRNQEGRF
AGCNRVAEQM TGKTEQELIG LTPHQVYDEE LASQVVASDH EVLENDVSVT EDLWLRFADG
RRRYFEMRKV PFYSADGTRL GVLAFGRDTT ERKQAENAVN KASKDKTAFI ATISHELRTP
LNGIVGLSRM LRDTNLTSEQ FAWVSTIYAS GITLGNIFND IIDLDRLDRD RLELSLKTVS
IKDFTQELGS IIELLADDKE LTFAAHVEDP MPALVEVDGT RLRQILWNLL FNAVKFTQKG
VVSLEVKAKA IDAETSMVTF KVCDTGVGIP PQELDKVFAM YYQVNLPEHQ SATGTGIGLA
ICQQMVSLMN GTISVSSVVG EGTCFTVDLP LEISKKPIQV ETLKVTGLQI LLVEDIELNV
MVAKALLEKL GQHVDVAMTG NEAITMARDK QYDLILLDIQ LPDMNGFEVA NVLHDESLVE
QTSIVALTAN VIKTRQEYLD NGMDDVIAKP VKKSRIIEVF NKLFCEQPSE PHQPAPEPKK
DHLNTILDLE LLQMLVDTIG HEMVRTSVKV FQEKIPEYLE ILQISLSADE KDEVCSQAHK
IKGAAGSVGL ARVQKIANEI QQGDHPAWWQ NVHDWVEQLN QAANQDLQKL INWLSQQDID
D
//
