ID A0A1V2B1X3_9BACT Unreviewed; 669 AA.
AC A0A1V2B1X3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BW716_20795 {ECO:0000313|EMBL:OMP77259.1};
OS [Flexibacter] sp. ATCC 35208.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=1936242 {ECO:0000313|EMBL:OMP77259.1, ECO:0000313|Proteomes:UP000188534};
RN [1] {ECO:0000313|EMBL:OMP77259.1, ECO:0000313|Proteomes:UP000188534}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35208 {ECO:0000313|EMBL:OMP77259.1,
RC ECO:0000313|Proteomes:UP000188534};
RA Webster A.L., Walker C., Li H., Skinnider M., Magarvey N.A.;
RT "Elucidation and Expansion of Monobactam Biosynthesis.";
RL Submitted (JAN-2017) 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: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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:OMP77259.1}.
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DR EMBL; MTKN01000034; OMP77259.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V2B1X3; -.
DR OrthoDB; 9781208at2; -.
DR Proteomes; UP000188534; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000188534}.
FT DOMAIN 166..387
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 411..529
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 565..661
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 139..166
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 460
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 604
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 669 AA; 75849 MW; C09D64058D65B377 CRC64;
MARIKGTRKH PITRSISPPD IFSLPISVYF QHTNAGILLL DAEQHIVWVN AVFQQYTGED
IDLVPDLPFA TIARYLARGA RNPEAFLATV EDLLTQKNPY FGQELLFSDG RIFELNYTPL
WHNGVFNGSM WQVTDISGRQ LQQATLEQAR QQAEEARGAQ KEFLASMSHE IRTPLNVIIG
MTHLLEETNL DGHQQDYINI LKHSSNILLG LISDILDISK IEAGEFQVNQ REFNLTALVQ
SLRHTFELKL GQRPVKISAT IDPRIQNRLV GDDTLLNQIL MNLLGNAEKF TPEGEIAIRV
TPESWQDDKV WVRFRICDTG IGISKDKLEL IFKNYKQAEQ EIREKYGGTG LGLAISKQLI
ELQGGTICVE DTPGYNTCFS FNLPFIDTRK SAVTTPGAGA RRKQASFSGS SVLVIEDNAM
NLHYINSLLE KYNVEHQLAT NGPDALYFLN SRQYDLVLID IRIPGLNGLE LAGRIREDED
KPNVATPLVA TTALAMESTF TQARQAGITD ILTKPYTPDQ LLQVLNKYLN EDETELIMEE
TNNTSGFEFH KDLDVKYLNT LYENNISYAA DLFEIFLKTI REELVKIQAL VNARDWELLK
FQVHKLKPNF SMVGLTWISA RMQNLENTLN ANTALPPEEV DALFANISEE VEKFYPIIEA
EYDRMKIYQ
//
