ID I0TAU3_9BACT Unreviewed; 1170 AA.
AC I0TAU3;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=HMPREF9969_0210 {ECO:0000313|EMBL:EID32746.1};
OS Prevotella sp. oral taxon 306 str. F0472.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1095752 {ECO:0000313|EMBL:EID32746.1, ECO:0000313|Proteomes:UP000004421};
RN [1] {ECO:0000313|EMBL:EID32746.1, ECO:0000313|Proteomes:UP000004421}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0472 {ECO:0000313|EMBL:EID32746.1,
RC ECO:0000313|Proteomes:UP000004421};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (MAR-2012) 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:EID32746.1}.
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DR EMBL; AJIN01000061; EID32746.1; -; Genomic_DNA.
DR AlphaFoldDB; I0TAU3; -.
DR STRING; 1095752.HMPREF9969_0210; -.
DR PATRIC; fig|1095752.3.peg.1931; -.
DR eggNOG; COG0457; Bacteria.
DR eggNOG; COG4251; Bacteria.
DR Proteomes; UP000004421; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR033405; DUF5112.
DR InterPro; IPR033406; DUF5113.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF17139; DUF5112; 1.
DR Pfam; PF17140; DUF5113; 2.
DR Pfam; PF02518; HATPase_c; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00028; TPR; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50005; TPR; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 393..415
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 865..886
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 297..330
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 479..698
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 1170 AA; 134740 MW; DE940E58D5694E48 CRC64;
MSLAAICLLL FFSACDAPHR QQVDDYNDKA YAAHYRNLDS VKIYAKQALA LSNGYNTGKA
EALNNLAFVY LMQMHFDKAY ATLNEVMGST DDQVELLVAD IQMMRLCQRE SNNKEYYDYN
EEANKRFLRI NEDKRLLTDR QRRRMVYARS EYAIVSSTYY YYVGLEQPSV RALSAINPDG
EIQTDMPQLL AYLYNVGAGG IFTKGKQEEI NQKEFDYLIR CYMLAIHHNY PYWEANSLQA
LSEHLVNDKS REALIRDNLP SFKYLKVGNL PDSLIAGNLA ERSLSIFQKY GDVYQTAGSY
RTLASCYWQI KDYRSALICL QNALKQNPAI NQAPDLVASI REQLSVVYSA MDNKQASDYN
RNIYLDLQEQ TRQDRYYEAR ADQLDSTSQQ LNIMIIAIGL IIIVILSLLI IFHYLRRRAD
NQSELNKLLL PLEEWKHHNV AYMAQLDDEY TEISEQLTIS NIHLIDNKRR YLEQRAKVSL
VNSIMPLINR MLHEINKLKR GGESEAVRSE RYTYIRELTD MINDLNSTLT EWIQLRQGRL
SLHIESFPVQ QVFDIVKKGR MAFQLKGVQL KVEDTTAIVK ADRILTLFMV NTLADNARKF
TPAGGKVCIK AVEEADYVEL SVEDTGCGIN EETQQHLFDR KPIHDQKDST SHGFGLMNCN
GIINKYRKIS QIFTVCQIGV KSEENKGSRF FFRLPKGVSR VLLFLLIAFS SLCTAQARPQ
RDNDKAAAIA RKDYMTLAGI YADSAYFSNI NGQYEQTLRF ADTCRYYINQ QYHKLYPHGK
LFMQRIGSLS NVAAEIKWFH ADVPVDYRVI LDIRNESAVA ALALHEWDLY KYNNNVYTHL
FKERSADSSL GEYCRMMMKS ETNKNVAIAL LVLLLLSILP VYYVMYYRHR LTFQFCIEQI
KHINAVLLSD VSVEKKLKEV DRVNSDRLPE RLRNIVQQIR EALVASQEAS QKSKADIEAL
EDEVHCVEYE NERLHISNSI LDNCLSTLKH ETMYYPSRIR QLVETDTDSQ LEAIDELAVY
YKELYSLLSQ QAMHQVRAIK LMAKSVDIAT LVPENKFKQP LAPIPPVAGD PVMIAYLFDI
LYSENQNQPL RITAEEHQKQ YVILHVLLSS MHLSAEECRE LFSPQAQGMM FFSCRQIVRD
NGEATNRRGC GIIAKPTEEG TEIQITLAKA
//
