ID A0A1F3NUI4_9BACT Unreviewed; 1138 AA.
AC A0A1F3NUI4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A3G23_06120 {ECO:0000313|EMBL:OFY69121.1};
OS Bacteroidetes bacterium RIFCSPLOWO2_12_FULL_37_12.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1797365 {ECO:0000313|EMBL:OFY69121.1, ECO:0000313|Proteomes:UP000176497};
RN [1] {ECO:0000313|EMBL:OFY69121.1, ECO:0000313|Proteomes:UP000176497}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OFY69121.1}.
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DR EMBL; MEPC01000038; OFY69121.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F3NUI4; -.
DR STRING; 1797365.A3G23_06120; -.
DR Proteomes; UP000176497; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR InterPro; IPR011110; Reg_prop.
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; PF07494; Reg_prop; 7.
DR Pfam; PF07228; SpoIIE; 1.
DR Pfam; PF07495; Y_Y_Y; 1.
DR SMART; SM00331; PP2C_SIG; 1.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 3.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 829..847
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 909..1138
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|SMART:SM00331"
SQ SEQUENCE 1138 AA; 130161 MW; 2B42B0083850E0C5 CRC64;
MKFLKIINFI VALCFFVLVA IPHFNAQTYS FQTFNVQQGL AQSQVYAICQ DKSGNLWFGT
MGGGVCRYDG INFETFTVRD GLIDNTIYDL FPDTSGGVWI GTQQGITHYL PPDQLNVSGA
KTASRSKPVF INYNKENGLA SLQILSLYLD KGNNLWAGTY NGVSKLPAET IQLTETPDYP
KEKRTELFKN FTVKQELLDS LVLSINEDNL GNLYFSSTKG VNIMKHLLRK VDKDQAKKFI
LYFDKIVKED GIISDRIYHV VKDKIGSIWL VSQVGFTRID PETSRKLGHY VFHNFSIGKE
TFRGERVTAF IQDLRGNYWV ATSGQGLFRV DMDENSGKVK VLENITTRNG LPTDDLFGLF
EDREGNLWIG TDGGGVTRFR GKMFESFSKE DGLNDNTVFS ILQTKDEKFW IGSYTGGLNI
YDPTAELTKR FSVFQFPKNL ITNSVSHITE DSYGNIWIAG DIGTIQYKPM FGTGEKAFKL
FTTLDTISYY KHSNKIIEDK FKNIWIAFMY RGLLKLTPDS SAPQGYKRKF ITPKDGLVKQ
FVRDFIIDHN GDLWAGTSKG LSHVILKSDT SKPEVHKITK EIGLPCEYIL ALFEDRKNNI
WLGTKEGAIK IVRNPDELKA GEQSKYVFKK FSTTDGLSSD LIYLINEDSE GNLWFGTNKG
VDQYIVDRGT FRNYGKAEGF TGIETNHKAT CKDKDGNLWF GTIKGVIKYN PKEVIMNSAE
PLTRINRLRV YFKDVEIPAD HVFRYDQNYI TFDFVAVSLT VPEKVRYQWK LQGFDNDWLP
VTNETRVTYS NIPHGEYIFM LRAANNDGLW NEKPVTFSFI VTPPFWKTWW FYSGCAVFLM
LCMYGYIKWR EKKLIKEKAV LEAKVTERTN ELSEANSLLS EKNRKITQSI NYARRLQKAI
LPPMELVHEY FPESFILFKP RDIVSGDFYW LDVKGNSILF AAADCTGHGV PGAMMSIVGY
NLLNQSASSG NGDLIPEPSG ILQNLNTGLG KIFREDFEES DMRDGMDIAL CSFDRQTMKL
KYSGAYNPLY LIRNQELIIK TANKFPIGKY LGKKRQLFTS HELDVLNHDT IYIFSDGYID
QFGGPDNRKF MRTRFQKMVL EIQKLSMEEQ KEYLDQVIEE WKGDRKQLDD ILVIGVKI
//
