ID A0A1T1CCR4_9FLAO Unreviewed; 1330 AA.
AC A0A1T1CCR4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BXU11_12750 {ECO:0000313|EMBL:OOV26351.1};
OS Flavobacterium sp. LM5.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1938610 {ECO:0000313|EMBL:OOV26351.1, ECO:0000313|Proteomes:UP000189962};
RN [1] {ECO:0000313|EMBL:OOV26351.1, ECO:0000313|Proteomes:UP000189962}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LM5 {ECO:0000313|EMBL:OOV26351.1,
RC ECO:0000313|Proteomes:UP000189962};
RA Hentchel K., Vargas G., Fiebig A., Chen S.L., Coleman M., Crosson S.;
RT "Genome sequences of bacteria isolated from the littoral zone of southern
RT Lake Michigan.";
RL Submitted (JAN-2017) 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 -!- 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:OOV26351.1}.
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DR EMBL; MUFX01000004; OOV26351.1; -; Genomic_DNA.
DR Proteomes; UP000189962; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd00130; PAS; 3.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 2.
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; 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; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR43719:SF28; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK2; 1.
DR PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 3.
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; SSF55781; GAF domain-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 70..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 97..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 127..144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 172..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 197..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 225..269
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 335..393
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 405..457
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 809..883
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 954..1176
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1208..1326
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 1259
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1330 AA; 153978 MW; B355DEFD48199B7E CRC64;
MQNLILPHGS FFLWSIEFKN ILASENQQLI QLTVFFILIA LSFPIYSTFK KLKTDAIHQG
EVTSQKEFHF YILLFGALII LLELLFDIFK IRPKSLLVQN TLVAFVMLLT YFFCTKLSFV
KNNMKKVFSF TFIFYFGVVL INVFSHDNDF IPKVAFSILL FLSFDVLKNT KLYWYFIGSV
LLLVSLFTLF HFTPSPLGAY LFSCTFIITI INYFRKKIDK SQTKENNFIK EIVNNGNSLT
VACNYHGEII YCSDTIASIL GYSPKEVMGF EFWKLTEDPE FVGLTYHNEF LDGQIYTRKL
KCKDGSYKYI QWTDKKINNN IIIGIGQDIT EQKRLHDQYK NIILNANDLI FEVNIHGIFT
FINDFSIKTL QYEENILLGK NYISIIREDY HEEIMNLFVK KKKISVIEFP IKTKFNDSIW
ISLKIIIQKD DNGKIIGYSG IGRDITNIKL NELKNTERQQ KIALYNETIK NLFTVNFRDF
DKIENAIQHI LATAATISQC DRVSYWKYRE KTIVCESIFF LNTKTFGKKI ILKKENYPIH
TKKIKQGLQL YKNDTNQKTD NLEFYDSYYS TNAIKSIIDT PIFLNGELLG VLSFETTAEK
RNWDQEDLTF SRTIADILSI AIATHKQFEA EKKLQKKSDL LAEMSLCTEK FLLSKSLDEM
FTDTFEIMGN ATQVDHLFYY EKEMDTQLFS QKFKWARKGI PLQITKTKQL TEENLIEIIV
KAKKKKTFKS TISKLKDSFF KKLLIANEIK SILIVPLLFK DNFIGFIGMD DCSMERNWTK
EEIFILKTLA SNISYALERD RNEKLILKSE EKFKLIANNI PGAVYLSKYD ELATKVYMND
TIEKITGYSK SDFLEQKISL ITLLHPEDKQ LILEHKNKNF NNGKPYHDRY RIQTKKGNYV
WIEEFSDAIR KDNKIEYIGG ILFDISEKIE NEVIIKEKQL AEAANKAKSD FLANMSHEIR
TPLNGIIGFS DLLIKTHLNR TQEKYMTTIN QSALSLLDII NDILDFSKIE AGKLELFIEK
QELTEILNQT IDLIFFESNQ KKLELYLKIA PEVPKFVWID SVRLKQILIN LLGNAVKFTE
KGSITLSVSV QKEINTTNHT LRFSIIDTGI GILEKNKKKI FSAFSQEDNS TSKKFGGTGL
GLTISNQLLG LMNSKLNVES KINVGSTFYF DIDLETSNEI EIAEPKTDSK ISNFSGAISK
KHAIPNLKIM IVEDNKINML LLKTILKNLF VEVEIIECLH GKQAIEQLEN KQPNLIFMDI
QMPIMNGYDT TKAIRKILNG KYLPIIAITA GTEKEERRKC LKVGMDDYIP KPIIKGVIEE
VVLKWLNKNN
//
