ID A0A223NTG5_9SPHI Unreviewed; 906 AA.
AC A0A223NTG5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-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=MuYL_1287 {ECO:0000313|EMBL:ASU33185.1};
OS Mucilaginibacter xinganensis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1234841 {ECO:0000313|EMBL:ASU33185.1, ECO:0000313|Proteomes:UP000215002};
RN [1] {ECO:0000313|EMBL:ASU33185.1, ECO:0000313|Proteomes:UP000215002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BJC16-A31 {ECO:0000313|EMBL:ASU33185.1,
RC ECO:0000313|Proteomes:UP000215002};
RG Henan University of Science and Technology;
RA You X.;
RT "Complete genome sequence of Mucilaginibacter sp. strain BJC16-A31.";
RL Submitted (AUG-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP022743; ASU33185.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A223NTG5; -.
DR KEGG; muc:MuYL_1287; -.
DR OrthoDB; 9813151at2; -.
DR Proteomes; UP000215002; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ASU33185.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000215002};
KW Transferase {ECO:0000313|EMBL:ASU33185.1}.
FT DOMAIN 325..383
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 637..689
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 693..906
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 129..247
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 374..401
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 906 AA; 101619 MW; 14F7445EC4F5D25E CRC64;
MNTQSHRFSN EKLLEILALS QNATAIYTGE EITIQAANNV MIGFWGKDRS VIGKPLAEAV
PELVGQPFLD ILREVWRTGI TYEAKDAEAL LLVDGKLQTF YFDFVYRAIN NEAGEIDCIL
HTATDVTELN LGRNLVAHAK EQQEALEREQ VLNQELGTSN EELSAANEEL AAAMEELSAT
NDELQLTKDS LQALNDELER RVAERTKKVE DLYQELETLN KELRASNEEL VNANEELSVS
RESLEKLVVE LAGSENRTRS IIEAAPFPIG VYTGREMRIT FVNKAITDVW GKGDNLTGRL
YAEVLPELDN QEVFKQLDDV YTSGISFEAR NQRIDLAVEG ELKTFYFNYN FTALRNEAGE
VYGVMNTAAD VTDVVVAKQQ LEKYAYELAS LNEELTASNE EQVAVNLELK LLYEKLKISQ
DEQHELINEL SASERKFRTL IKKAPVAINV FRTRELIIES VNDKMLEIWG KTDGVEGKTF
TEALPEIANQ PFIEILRAVF ETGEPYYGLE NKAVIIKDGI PEDRYFNFIY QPIAEKDGSV
GSVLQVVTEV TDQVNSKREI AEVNTRLNIA IEAGGLGSTE VDLATGKMEC NEQFKKYFGR
TSDQPFTYTD LFEAMLPQYR KKVKALVATA IEKNSLYESQ YEVAWPDGSI HWISAHGRAR
YDNNGNAIKM VGIISDITEA KADEQRKNDF IGMVSHELKT PLTSLTAYMQ ILQAKARKNS
DNFASGALDM ANKQVKKMTT MINGFLNVSR LESGKIHIDS QRFDMAGLVK EIEEESAVTI
TSHNVIFAPV EETPVYADRD KIGQVINNFI SNAVKYSPMG STIHIACLSG DGSVQVSVQD
EGRGISPEDQ QKLFERYYRV KDQPATISGF GIGLYVCAEI INRHNGNIWL ESEPDKGSTF
YFSLPV
//
