ID A0A087CR62_9BIFI Unreviewed; 681 AA.
AC A0A087CR62;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BREU_0940 {ECO:0000313|EMBL:KFI85762.1};
OS Bifidobacterium reuteri DSM 23975.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437610 {ECO:0000313|EMBL:KFI85762.1, ECO:0000313|Proteomes:UP000028984};
RN [1] {ECO:0000313|EMBL:KFI85762.1, ECO:0000313|Proteomes:UP000028984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23975 {ECO:0000313|EMBL:KFI85762.1,
RC ECO:0000313|Proteomes:UP000028984};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) 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:KFI85762.1}.
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DR EMBL; JGZK01000006; KFI85762.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087CR62; -.
DR STRING; 1437610.BREU_0940; -.
DR eggNOG; COG2770; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR Proteomes; UP000028984; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003660; HAMP_dom.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR45436:SF5; SENSOR HISTIDINE KINASE TRCS; 1.
DR PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFI85762.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000028984};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KFI85762.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 68..87
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 288..311
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 312..365
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 380..653
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 681 AA; 73177 MW; 0925FA0E904DDC5B CRC64;
MTSPEKSPQP VSPASPAVSG TKSSMANTST DSSPRVNVPG LQYLKEHHER KRNVFLRHLD
RVSLSGKLVA CTIVVLLVGV TVISFSIRTL VGNYMMEKVD TQLRVQSQLV FNNIDLLAKD
DNSNGLTSPN SYFLQLQYTD GTKDADGDPL TVTPLLPQLK DGLVSIPVLP SDGDTSGITL
GQVFTAPAVA KQIVQVQSDT AQSPAQGDAS GGGGTDGSDS SQSTSRVTTV LTDPRNNVSH
ATLASANSPW RVLPMQWTER DSKGVEKIRG VMYIGLSLSD QIDTLNTLTR YCVVVGIAVL
LLGGSLSTLI IQQTMTPLKR MEKTAAKIAA GDLSQRIPSA PENTEVGSLA ASLNTMLTRI
EVSFHEQEET TEKMKRFVSD ASHELRTPLA AIHGYAELYK MQRDMPGALE RADESIEHIE
RSSQRMTVLV EDLLSLARLD EGRGIDVTGS VNLASLVTDA VDDLHALDPN RTIMRNRLAL
APGRDMSHPA SLQLADGGWE AVTLSGDASR LRQVVTNIVG NIHRYTPADS PAEVAIGTMP
AAIDPRQLSQ MPTTEASMRR FIDAAEVGAS MQTGYRYAVL QFVDHGPGVP PESRSKIFER
FYTADPSRAR QKGGTGLGMA IAQSVVKAHH GFICATGTEG GGLTFTVILP IERMASAPAG
HQTQTKPAKT KTSWFSGERK A
//
