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Database: UniProt
Entry: A0A0M2XT30_9SPHI
LinkDB: A0A0M2XT30_9SPHI
Original site: A0A0M2XT30_9SPHI 
ID   A0A0M2XT30_9SPHI        Unreviewed;      1393 AA.
AC   A0A0M2XT30;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=AAW12_21595 {ECO:0000313|EMBL:KKO88794.1};
OS   Sphingobacterium sp. Ag1.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=1643451 {ECO:0000313|EMBL:KKO88794.1, ECO:0000313|Proteomes:UP000034524};
RN   [1] {ECO:0000313|EMBL:KKO88794.1, ECO:0000313|Proteomes:UP000034524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ag1 {ECO:0000313|EMBL:KKO88794.1,
RC   ECO:0000313|Proteomes:UP000034524};
RA   Pei D., Yu W., Kukutla P., Xu J.;
RT   "Draft Genome Sequences of Sphingobacterium sp. Ag1 from Mosquito Anopheles
RT   gambiae.";
RL   Submitted (APR-2015) 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:KKO88794.1}.
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DR   EMBL; LBGU01000044; KKO88794.1; -; Genomic_DNA.
DR   PATRIC; fig|1643451.3.peg.278; -.
DR   Proteomes; UP000034524; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd17574; REC_OmpR; 1.
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; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR018060; HTH_AraC.
DR   InterPro; IPR018062; HTH_AraC-typ_CS.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR011110; Reg_prop.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR011123; Y_Y_Y.
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; PF12833; HTH_18; 1.
DR   Pfam; PF07494; Reg_prop; 8.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF07495; Y_Y_Y; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00342; HTH_ARAC; 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; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1.
DR   PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..1393
FT                   /note="histidine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005647161"
FT   TRANSMEM        810..831
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          864..1090
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1136..1251
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1282..1382
FT                   /note="HTH araC/xylS-type"
FT                   /evidence="ECO:0000259|PROSITE:PS01124"
FT   MOD_RES         1184
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1393 AA;  157850 MW;  40A6EB69C7D2FFD4 CRC64;
     MPLRVFVRCF CCALALISVL YAQEKNYRFL HLDVNEGLSQ GSVFAIAQDY LGFMWIGTRD
     GLNKYDARKF TIYRSNPQDS LSLEHNFIQA ITEDNKRRLW IGTMTGLNLY NRASDNFIRI
     PLPTVESSSG KMDVNVHQIF QDSKGKIWIA TNIGLYKIKE GRHLEAELVF NEITVERSQG
     KEYYRNFRTV YEDRRKRLWF CTDDAIVLMQ AASKDGNSLK VLRTYFKEKS VDNKVNQRFQ
     AVLEVSPGIF WVGTKYNGIR IINENTGEIS SLTEAGNHTG LASQDVRSLK KTVDGKIWIG
     TFNGLYVYQN GKLLFIQADD GNPNSLSNNS IRPIFQDKRG SIWIGTYFGG VNIYDKDIPN
     FQNFTHQAKR NSLSYNVVSA FVENGMGELV IGTEGGGLNY FNRRTNSFFS ERHDKNNLNG
     LSHNNVKSIC LDKEGNLWVG TYDGGLNLRR KGQQGYEHFR FDPNVSNGLA NNNVYAILED
     RNGDIWIGTF GGGLQVLRKN QKVGSFQTFD VAGKQLSSNM VRALLEDSKG NLWIGTSNGL
     NLKLAGTDKF VSFLNDKKDS LSISGNDIVS IHEDRKGQIW IGTYMGGLNR YLPEKKAFKR
     FNERNGLPIN NVFAMLSDLK NKLWLSTNTG ISCFDPLSGH VRTYTKTDGL PGNEYIQNAA
     AMLRDGKLAF GSFSGFTLFN PDSLSVNNYI PPIQFTELKL FNKTVLPGID AVIPKDISMM
     DELILDHNQN VFSLEFSVLN YVHPEKNQYA YYLKGFDQDW NYVSNPVATY TNLDPGTYEL
     WVKGANNDGV WNEKATVLKI KVLPAPWKTW WAYSGYFLLF AAAGFLIIRF FHGRNKLKQD
     LLIRQIDSEK QEELHEAKLN FFTNISHEFR TPLSLIIGPL NQLKGDRSLS AYVQEHLGYA
     TRNADRLMNL VNQLLDFRKH EGGKMKLFCQ KVHLATYLEN IRQNFHFIAE KNNIQFFLDN
     KVSPNYVAGF DPEQFEKVLV NLIYNAFKFT DKGGKIKIQV ELEGEGELEK LLVSVWDSGR
     GISPKDIPFV FEQFYQANTK GLSATNGGIG LALCRSIVQL HGGKLTVESN MAQETTDYNT
     VFRISLPQSA VVIEELPVLT DTPGMICADP ADAGMPYVDT TKTAIERPAA EEDKPIILVA
     EDNVELRCFL CENLRKKYIV LEANDGIEAL ELVQTKQPDI IISDVTMPNC DGITLLQQIK
     NDSSSNHIPV ILLTARTADP YITEAFEIGT DDYITKPFSM PHLIQKISNI LQTRKRLEEK
     FVQHYLLGAQ GTDLPERTRF LDQVLKIVEE NLGCEDFGVL DLTKAIGVSR SVLYRKIKQQ
     TGLNLVEFIN MVRLKKAAYI LVNDTGLSIS EVAYQVGFND PKYFSKSFKK FYKESPRTYV
     EKFGVKESSN LEK
//
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