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Database: UniProt
Entry: A0A1G6AHU8_9FIRM
LinkDB: A0A1G6AHU8_9FIRM
Original site: A0A1G6AHU8_9FIRM 
ID   A0A1G6AHU8_9FIRM        Unreviewed;       605 AA.
AC   A0A1G6AHU8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN02910298_00287 {ECO:0000313|EMBL:SDB07965.1};
OS   Pseudobutyrivibrio sp. YE44.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Pseudobutyrivibrio.
OX   NCBI_TaxID=1520802 {ECO:0000313|EMBL:SDB07965.1, ECO:0000313|Proteomes:UP000198713};
RN   [1] {ECO:0000313|Proteomes:UP000198713}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YE44 {ECO:0000313|Proteomes:UP000198713};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; FMXT01000001; SDB07965.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6AHU8; -.
DR   STRING; 1520802.SAMN02910298_00287; -.
DR   OrthoDB; 9809348at2; -.
DR   Proteomes; UP000198713; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd12912; PDC2_MCP_like; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR033479; dCache_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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR   PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR   PANTHER; PTHR34220:SF7; SENSOR HISTIDINE KINASE YPDA; 1.
DR   Pfam; PF02743; dCache_1; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF06580; His_kinase; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SDB07965.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        21..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        303..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          325..378
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          485..593
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          366..398
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   605 AA;  68734 MW;  658E36A084A61A70 CRC64;
     MKSIDFYNQY KRVRRASKRR SIQLIISLSF TIVSILSMAF ITMAFYTTYI NTARETAIEN
     NKQVIDQMSW TLNSYLRNMM GVSNSMYYGV IKNMDLTSDT MNKEMDILYE ANKDDLISIA
     CISQDGALIS AAPISTRKSG VDFTEQEWFT STEEKIENFH FSKPHVQNMF EGSNYRYYWV
     VSLSRSVDLN YMGYARRGIL LVDMNYSAIE QMFSRVNEKG SGYVYLIDGD GEIIYHPKQK
     AISGGLMQEN NIAAAEYDDG GHMENFEGSE RAVVVKTIGY TGWKIVSVVP ASELSAPYNQ
     LRAFMMIIVT VTIFLIVFGN IIISKIVTDP IRQLEASLKS IEEGSLEAQK VYIGGSHEIR
     HLGRTIRSLV VQMRDLMDER VKEQKEKRKS ELNALQAQIN PHFLYNTLDS VIWMIESEKY
     PEAISMITSL ATLFRISLSK GNNIITIKDE ITHARNYLAI QKVRYKNKFD ANIDIDPAIE
     DCVTIKLIIQ PLIENAIYHA VGDLDDEGII DIKGYEKDGD IFIEVRDNGM GIPPDVLENL
     LKEKSQSKGK GSGIGLWNIN QRINLYFKND YGLKLESELD EGTVAIIHLP KMTMEEYLGG
     EGNAK
//
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