ID Q5NY08_AROAE Unreviewed; 1015 AA.
AC Q5NY08;
DT 04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT 04-JAN-2005, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ebA6890 {ECO:0000313|EMBL:CAI10056.1};
OS Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Aromatoleum.
OX NCBI_TaxID=76114 {ECO:0000313|EMBL:CAI10056.1, ECO:0000313|Proteomes:UP000006552};
RN [1] {ECO:0000313|EMBL:CAI10056.1, ECO:0000313|Proteomes:UP000006552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EbN1 {ECO:0000313|EMBL:CAI10056.1,
RC ECO:0000313|Proteomes:UP000006552};
RX PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA Reinhardt R.;
RT "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT bacterium, strain EbN1.";
RL Arch. Microbiol. 183:27-36(2005).
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};
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DR EMBL; CR555306; CAI10056.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5NY08; -.
DR STRING; 76114.ebA6890; -.
DR KEGG; eba:ebA6890; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_011598_0_0_4; -.
DR Proteomes; UP000006552; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
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; 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; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000006552};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 48..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 81..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 216..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 409..461
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 487..558
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 561..612
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 637..856
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 881..1000
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 934
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1015 AA; 109403 MW; C44D4DD01A220F07 CRC64;
MAISWPSLRE GDARPETMPM TIRMGDSVFL PAAAERVPSV WGMRLRQISA YASPAVVVLA
LIGAVGWFVG MPALGTLGAE FVPFLPTSIV KLLFIAFALR ELDRAPAARA RFTVAFAAVA
VALMSMMALT IGPDPVGMVL SPLLPPAESE SIYSPSGPAV GTATTYLLLS AALALAPLSD
SRLVAISRLL AVAVGGVALV AVVGLTFHFV RLNLAIPSVG IALPVALALL ITSFSLLLRN
PPPRFIQLLE HDSPGAVIFR RLLPVAIAVP LLAGWLQALG QRFGWFGVIE GEGVVAVAMI
VACTVLILWT AARLDEMNTD RSIAEIRANT QQQWLEVTLA TIEDAVITVN NEMRVGFLNP
AAETLLDVKV GDAIGRDLQE LVVLVDEATD QPMGSPFARA FSELGQVTIS GEPGLRMRDG
SVRAVEATAT PIRDWKGGIN GGVLVLRDAR AHRAREHADR QAYAALDRRV GDRTRALERT
MSVLRESTTL LRTIAASTPE LIVAKSREGR IMMVNPAALQ AMGLSRAQVV GHKEESLFGS
SEEMRRILEN DRRVIETRRP IVVEESRTTR AGTRTFLVTK SPLRDSQGHV FGLVGVSKDI
TERKRAQREL EQLLVAEHRL RGEAERANRA KDEFLAIVSH ELRSPLNALK GWSQVLTASG
NPEPATVLRA AEAIKRNIDH QARLIDDLLD TSRIISGKLE LNSRRVNLVE IVHAAIDLSW
DTAKAKRIEL RVDTACPSLM INGDHDRLQQ IVINLLANAL KFTPEGGWVE LRLAQGETSV
ILSVADSGVG IEAGFLPHVF DRFSQADTSM TRRHQGLGIG LALVRNLVEL HGGAVRVESA
GPGCGSVFTV ELPRPVQDAL PGESPEAREG RPPRIALEGV DVLVVDDEAD AREVMTLILS
QAGAHVRTFS SGTELLAELA RPDAVSLPAI LLLDIAMPGD SGFSVLQRVR ELASLPFIPA
VAVTALSRLD RTRFELAGFQ ECVGKPVEAR ILIETIAATL DVADLDAQRR QASAA
//
