ID A0A166UGL7_9GAMM Unreviewed; 1846 AA.
AC A0A166UGL7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=N475_24275 {ECO:0000313|EMBL:KZN30645.1};
OS Pseudoalteromonas luteoviolacea DSM 6061.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1365250 {ECO:0000313|EMBL:KZN30645.1, ECO:0000313|Proteomes:UP000076643};
RN [1] {ECO:0000313|EMBL:KZN30645.1, ECO:0000313|Proteomes:UP000076643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6061 {ECO:0000313|EMBL:KZN30645.1,
RC ECO:0000313|Proteomes:UP000076643};
RA Vynne N.G., Mansson M., Gram L.;
RT "Comparative Genomic and Metabolomic Analysis of Twelve Strains of
RT Pseudoalteromonas luteoviolacea.";
RL Submitted (JUL-2013) 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 -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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:KZN30645.1}.
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DR EMBL; AUYB01000148; KZN30645.1; -; Genomic_DNA.
DR RefSeq; WP_063366039.1; NZ_AUYB01000148.1.
DR PATRIC; fig|1365250.3.peg.4861; -.
DR Proteomes; UP000076643; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; 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; 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; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
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; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR011110; Reg_prop.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR011123; Y_Y_Y.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF07494; Reg_prop; 2.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF07495; Y_Y_Y; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 3.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF55781; GAF domain-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; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000076643};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 978..1054
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1058..1111
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1129..1351
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1366..1478
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1502..1618
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1659..1752
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 1099..1129
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1415
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1551
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1700
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1846 AA; 205546 MW; 1C12AD4F0DC2DDB3 CRC64;
MKPLRLLLVV VSSFVLVASK LCWAQIKVES ISAYNGLANP QIYAVSKDPQ GFMWFGSADG
VKRYDGYEFI SFNHDPNDPN SLSANSVGAL LFDKQGRLWA GTWGGGLNLF VREQQHFVHF
KHDPNELTSL GANKVQSLFE SRDGTLWVGT SGGGLNRMRE DGQSFERFVH VDNDPSSIGN
DRVWSISEDL NGGIWAGTSN GLYRLDRDTG KFQGFGVAEN SLDHAEVRQV SVDELGQIWV
ATRTSFGLFN PNINEYKTYN LPTGTLPSVT RLMHFNGDIL LATFAGIYRF SPRLEQFLSP
IPNSKLALLQ NRDVRQVLVD DSGLLWAATR YSGVQKVFPN PPAFMSWQDY LQDELLSGLF
NQVLTAEMAA QGGVWLGTGR GLVHFDGKET FIPFADAETL QGNYRLRIHS LARDEAGQLF
AGTSFGLYKV DELNKKLELV TLSWLQDSRR SVEHVSFDRA GEMWLVLSGR DGMVRWNRNT
DEKRNYIPQQ DLEFVFHDSE GQVWAGTDGE GVFRVDPSNG KFEQFTAYGN KVGPNGNYVT
HAMQQGNQVW LATNRGVTSF DLASKAFKQY VNTASQVNFA VKSIVSDEEG FLWFASASGV
FKFDPTYGIF HQFTTNDGLI NHHFLARSFV KFEDRILFGS IDGITGFNPK SVRVNTSAPP
VAFTQAFVDG KAIDIQSGRV LLNHNDKNLS IHFAALDYQA TGDNRYRTWL DGYHEGWSAT
TPDHTVNYRE LPPGEYQLKV QGSNNHGVWN QTGIELTIVS VPAWYQTLWF RITLPVLMVI
LLLFLFWLRV KQLRANSLEL EQKIARRTRD IVVLGEVGKE VAATYDMHVI SETIYNHLST
ILHCEFFAVG VFYEEQQYID YIYAMQQGEL YEALESHTKV VSSADVYCVA NGKEFYAASD
ESWQKMDLKA CNNLYGEQTK SVFCAPLVVE GKVLGVFTVQ SNKPRAYKEV HLNVLRTVAN
HIAVALANSL SYSELKEAEQ RLELAMQGAN AGTWEWDCQN DKLVTNTIWS TMLGYQEGEL
ELQYGETINR WRSLLHPDDL GHVEGALQAH LSKQSKTYRA EFRMKTADGG WKWILSMGRS
VNINQDSRRK EMFGIHMDIS DAKELETALK QAKERAESAT QAKSDFLSNM SHEIRTPMNA
IIGMSYLALE TQLNHKQRNY VEKIHRSAES LLGIINDILD FSKIEAGKLD IEHVEFCLEE
TIGSCLDVIS VKAKEKGLEL SAHIDAAIPS HLIGDPLRIS QILLNLGSNA VKFTELGGEV
LLDVRLESQF DGDITLKFAV IDSGIGMTSE QQAKLFASFS QADTSTTRKY GGTGLGLAIS
KKLVELMHGE IHCQSALDVG STFSFTLVVN DALKEPEALT EFDIKNALII DGNSSSSRNL
QSCLSRFEID AQCAVSFQAT DLVEQAGEKD AVFIDARIEN EIGLLKQLRA NGNETPCIVM
PLYEFQPIEA YLESFGSTTY LQKPFLPTAV YGCLQRVLGL QNDTVMTEGE LKSSRTSLAG
AHLLLVEDND LNQELAIALL TGQGISVEVA EHGAQALEKL ATNRFDGVLM DCQMPVMDGY
TATRKIREQA QYASLPIIAM TASVMMDNQE AALACGMNDI IGKPLNVEKM FATLQKWIVV
SNNSIQTAEQ PAERVNSESG YPIIEGIDNQ VAKSISQGDV ALFTRLLKRF SDKHQHFTQH
FDEALQEAST DPDAPMRCAH TLKGTAGNIG ATGVQAVAGE LESACAEGLP VEEVIERVHS
QLDPLIENIN LVLLGLSSEQ PELSNEIQVQ ISQEEIEQKL VTLTTLLADY DTDAIDLVGE
LLPVYQGTEF FDSFNKLNLL IDDYDFDAAN ELLTQIKPKL LVQEQA
//
