ID A0A285MUM4_9FLAO Unreviewed; 1321 AA.
AC A0A285MUM4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN06265377_1326 {ECO:0000313|EMBL:SNY99516.1};
OS Allomuricauda parva.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Allomuricauda.
OX NCBI_TaxID=1247520 {ECO:0000313|EMBL:SNY99516.1, ECO:0000313|Proteomes:UP000219048};
RN [1] {ECO:0000313|Proteomes:UP000219048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25885 {ECO:0000313|Proteomes:UP000219048};
RA Varghese N., Submissions S.;
RL Submitted (SEP-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; OBEH01000002; SNY99516.1; -; Genomic_DNA.
DR Proteomes; UP000219048; Unassembled WGS sequence.
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; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 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; 4.
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; 6.
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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}.
FT DOMAIN 820..1034
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1073..1188
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1220..1319
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1121
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1321 AA; 149541 MW; 53CF649EB5DDDB51 CRC64;
MEFTGLSTEL GLSNGRVTAI AQDSIGFIWI GTKNGLNRYD GKSFKVYSKS NSNLSENYIS
DILIDDIGRM WIATNGGGVN LYNLASDTFI SYEKSGSAEQ KLNSDVVNKM FKDSSGGIWA
ATDKGLSYFD EKGKTFVTYL NESVESYRTP RANDILCIYQ DKKGVFWIGT NGAGLFCFNK
EQKSFNKYLI TEKGSNSLPD YILDIISINS DSILLGTNGD GLVGIDQMKN SLFEVFDSSK
TVPAIVRKFW RDKESNIWLG TDGNGLYKLS PDCKILQHYL KDDRLSNSIK GNTVTSLFED
KQGNFWIGTA WRGLSVWNKG TENLNIFYSD GKGYDSNPVL SIFKKDAFLW LGLDGQGLNK
LNEDDLEVVK FSQGQFAGMR NYFVQCFEPA GGTQYWIGTF TNGLNLFDEG KGIVKKFKRE
KNNQNSLPFD DVRDIVVLPS GDLWIATWGG GLSYFDSGSE EFFNYRQGNS DRNYISSDNV
VSLLDDGAYL WIATQGGGLN KFYKDNGVFE NFQTIKGDST SIGNNYVYSI IKDEKNILWL
GTNQGISKFN KEDTTFKNFD IGYGLNSNTV VSILQDQSKI LWLGTKKGIF RFDPNTNSVQ
LVPNTNMEFH INSAFIDESG TAYFGGIMGI IAINTKIPLV SHEYSKLVFT DFKLFNKSQI
PASEGVLDQN MVINKNINLK YNQNVITFGL ASLQFPKSTD NKLEVLMEGF EKEWRLIGEQ
TTVTYTNLSP GKYVFKARPS SSNLENGTND VRSVQIEIEP PPWKTSWAYF LYALTFIALL
WSMRFYTLKW AEIKNNLRAE KLKREKEDEI HRLKQRFFTN ISHEIRTPLT LIMGTLNSLK
GNFNANEQNR INAVRHSASR LMTLVNELLN IRKLETGNIK LHISQNNLVT FMHEIFLAFS
QQAISKDIEY VFTPEDKTVL VWFDKVQLEK TVYNLLTNAF KFTPQNGRIE VLVGSKNNFA
KIMVKDSGTG IAEDKLPHIF NRFYQNEEAS DGEIGFGIGL SIVKDIIELH HGTIKANSTL
GHGSTFKIRL PMGKEFFDAS QLNFEAEDVE QIGTRSFVEG QAKHASIANK ETEILIVEDN
TYLRDFLSDL LSTEYKVVTA ENGKKGLDLA MEHLPNLILS DIMMPEMDGV TLCYTLKTNV
LTSHIPVILL TARDMVESIM EGYETGADDY LIKPFHEGVL RARIKNLLEV RKKLRDRYSK
ELLLNPKEIA LNSPDQQFLE KLQKVLEDKM SNPEFHIDEL ALDMAMSHSG IYKKIKALTG
MTLVAFIKDF RLKRAAQILK QHNFAIADVS FMVGYSDRKH FSQEFKKKFG KNPSEFSKDY
S
//
