ID R5PV99_9BACT Unreviewed; 1188 AA.
AC R5PV99;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-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=BN465_02106 {ECO:0000313|EMBL:CCZ12877.1};
OS Prevotella sp. CAG:1092.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1262919 {ECO:0000313|EMBL:CCZ12877.1, ECO:0000313|Proteomes:UP000017987};
RN [1] {ECO:0000313|EMBL:CCZ12877.1, ECO:0000313|Proteomes:UP000017987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:1092 {ECO:0000313|Proteomes:UP000017987};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-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:CCZ12877.1}.
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DR EMBL; CAZL010000394; CCZ12877.1; -; Genomic_DNA.
DR STRING; 1262919.BN465_02106; -.
DR Proteomes; UP000017987; 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; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000017987};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 408..429
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 717..736
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 894..914
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 496..717
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 453..552
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 972..1012
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1188 AA; 135763 MW; 92AB02E07AD55A6B CRC64;
MDTLLRLVHN IKLFGCSIWL VSLWSILLFS ACSSNDSDVA DKLNTLSYAY HYRSLDSTEV
YARKAFAASE SYNAGKAEAL NNLAFVNIAR MDYQKAAQQL DSAINITDNQ VELLVAEIQY
MRLCQRQSHN KLFYIHQEKA KKYLDRIIED KNLLNSHQLK RLIYAQSEYY INISAYYYYV
GLVEPSIETM KCIDPDGDIQ KDTAQYLNYL YNVGAGGIIT NADANVVANE EFNYLTQCYI
VASQRNYPYW KAQALQAISE HLLSPSTRQI LITNYRPFLD YINTDGMDYS LLAGNLAQRS
LNIFTEYKDV YQTAGAYRTL AGCYWEIDDY PSALICLNSA LEADTIINRA PDLVASIREQ
LCLVYSAQND KVNSDINRNY YLDLQEQTRQ DKQLEARAYQ LDKSSKTLNA MIVAVLFMIA
VVLFVLVYFA RKRKQKGATV DINELLLPLK KWNIENNKKL TDLDDKLEEV QEQTALVRLS
EEKNKQRNLE QRAKLALVNS ITPFIDRIIN EINKLNSRHE SVELREERLK YISELTDEIN
EYNNVLTRWI QMQQGRVSLR IESFSINELF DIVAKSKMSY SLKGISLCVE PSTAVVKADR
VLTLFMINTL ADNARKFTPV GGKVTIKAEE KPDYVEVSIS DTGCGMDENK LAHVFDNKHI
SDDGTTSAQS HGFGLLNCKG IIENYKKISR IFAVCDINAD SSVGKGSRFA FRLPKGVVRM
IMALMVMVFG FTMPAYSVGN DKVERNNKKP TISRLNTQEQ HLNDAARFAD SAYYSNLNGT
YAHTLACADS CMKYLNMHIY AHAKSKTDIP KMVLFTTSSA MPAEILWFHK EIESDYAVIL
DIRNETAVAA LALHKWDLYR YNNKVYTRLF HECYADASLP HYVQTMQKAE NNKWVAIVIL
VLLLISIPPI YYMVYYRHII YYKVCVERIH AINEILLGDG TDEDKLKCVE EFNSKTGNLG
IAVLDNVVDQ ILATLRANAE SSEHKAEXXX XSEHKAEQLE YAHDELRQAE RENNILYVDN
SVLDNCLSAL KHETMYFPSR IKQSIETKDC DIQVVAELVT YYKQLYSLLS AQAMRQIERP
YKVDRDTMRY LFDLLKKLNG GCKPDYQVKE KDSVYVQLAF AMTSLNITSV QAQQLFTPLT
LDVNFLICRQ IVRELGEVTN LRACGIVATA DNIIEITIPK AIWKNLIS
//