(data stored in ACNUC7421 zone)

SWISSPROT: Q3ILJ4_PSEHT

ID   Q3ILJ4_PSEHT            Unreviewed;       772 AA.
AC   Q3ILJ4;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   30-AUG-2017, entry version 90.
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:CAI85638.1};
GN   OrderedLocusNames=PSHAa0550 {ECO:0000313|EMBL:CAI85638.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85638.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85638.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- CATALYTIC ACTIVITY: ATP + protein L-histidine = ADP + protein N-
CC       phospho-L-histidine. {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
CC       group from a His in the primary transmitter domain, to an Asp in
CC       the receiver domain and to a His in the secondary transmitter
CC       domain. {ECO:0000256|PIRSR:PIRSR003182-50}.
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DR   EMBL; CR954246; CAI85638.1; -; Genomic_DNA.
DR   RefSeq; WP_011327251.1; NC_007481.1.
DR   ProteinModelPortal; Q3ILJ4; -.
DR   STRING; 326442.PSHAa0550; -.
DR   EnsemblBacteria; CAI85638; CAI85638; PSHAa0550.
DR   KEGG; pha:PSHAa0550; -.
DR   PATRIC; fig|326442.8.peg.519; -.
DR   eggNOG; ENOG410XNMH; LUCA.
DR   HOGENOM; HOG000272667; -.
DR   KO; K07648; -.
DR   OMA; AMLEQYI; -.
DR   OrthoDB; POG091H03T5; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0005622; C:intracellular; IEA:GOC.
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 transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   CDD; cd00130; PAS; 1.
DR   CDD; cd00156; REC; 1.
DR   Gene3D; 1.10.287.970; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR027460; ArcB_TM.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
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   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 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; SSF47226; SSF47226; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   SUPFAM; SSF55785; SSF55785; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   TIGRFAMs; TIGR00229; sensory_box; 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;
DR   PRODOM; Q3ILJ4.
DR   SWISS-2DPAGE; Q3ILJ4.
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR003182};
KW   Cell inner membrane {ECO:0000256|PIRNR:PIRNR003182};
KW   Cell membrane {ECO:0000256|PIRNR:PIRNR003182};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
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|PIRSR:PIRSR003182-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843};
KW   Transcription {ECO:0000256|PIRNR:PIRNR003182};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR003182};
KW   Transferase {ECO:0000256|PIRNR:PIRNR003182,
KW   ECO:0000313|EMBL:CAI85638.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|PIRNR:PIRNR003182}.
FT   TRANSMEM     27     48       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     54     76       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      148    201       PAS (PER-ARNT-SIM). {ECO:0000259|PROSITE:
FT                                PS50112}.
FT   DOMAIN      219    272       PAC (PAS-associated C-terminal).
FT                                {ECO:0000259|PROSITE:PS50113}.
FT   DOMAIN      283    503       Histidine kinase. {ECO:0000259|PROSITE:
FT                                PS50109}.
FT   DOMAIN      518    634       Response regulatory.
FT                                {ECO:0000259|PROSITE:PS50110}.
FT   DOMAIN      674    767       HPt. {ECO:0000259|PROSITE:PS50894}.
FT   COILED      124    148       {ECO:0000256|SAM:Coils}.
FT   MOD_RES     286    286       Phosphohistidine; by autocatalysis.
FT                                {ECO:0000256|PIRSR:PIRSR003182-50}.
FT   MOD_RES     568    568       4-aspartylphosphate. {ECO:0000256|PIRSR:
FT                                PIRSR003182-50, ECO:0000256|PROSITE-
FT                                ProRule:PRU00169}.
FT   MOD_RES     713    713       Phosphohistidine. {ECO:0000256|PIRSR:
FT                                PIRSR003182-50, ECO:0000256|PROSITE-
FT                                ProRule:PRU00110}.
SQ   SEQUENCE   772 AA;  86105 MW;  12502B41118D2E35 CRC64;
     MTDSSLSPWA RVLSSLITRF GEFKTAAICY ALLLAVSLVL SSMFYYVAVG EVNLVDILAV
     VFFTSVVSPL VISVLINSIR QLDASYAYLD SATKQEKLLN QTLKDNINRL NVEIDERKMA
     FHAKHRAIEE LRKEIAERKK TQQELAQQSM LQRSIVDSSP DLFYYRDNNG VFAGCNKMFE
     EVMGKTSDEL IGKSAEQIFP NQFLSEVLKT DKQVEQTHQA LTIDVQYDVG GETRWFELRK
     LPFINDKGKY IGLLAFGRDI TSRKEAAEAL ETAYKDKGKF IATLSHELRT PLNGIVGLTR
     MLLDTELNKQ QRSWCNTVFS SAETLGNIFN DIIDLDKIDR EQLDIATNAI NVSDFINDVV
     NFAGLIAEQK DLSFDIKRLG MLDIYAQLDP TRLRQVVWNL INNAVKFTHK GSVTLTCIRE
     NRDDGPWLTM KISDTGEGIP AEQLSRIFDM YYKAPDLKGT NAIGSGIGLA VTKALVDAMQ
     GIISVNSTEG EGSCFIVEIP LILCSAPTEN SYVGRSLNIL LVEDVPLNAE IATNLLEQRG
     HEVIWAETGE DALSFVETED DLDLILLDMQ LPDINGDEVA RQIRADSHFD KLPIVALTAN
     VRSAEQELEG ISIQGALAKP INTVKLDKIL ADLFGIKQTR SNEPQLKVST AALADINAHL
     LDVETIEDFV NSMGLVVFKR SSQLFEKLNP QYQQELLTSL NSGDREEYKS VAHKLKGAAG
     SVGLNDVQLH AKVMEYGALD KSDEVLKQWL DVLADKINEG QHALHLFLQQ LE
//

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