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Database: UniProt
Entry: A0A0M2XWI6_9SPHI
LinkDB: A0A0M2XWI6_9SPHI
Original site: A0A0M2XWI6_9SPHI 
ID   A0A0M2XWI6_9SPHI        Unreviewed;       509 AA.
AC   A0A0M2XWI6;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-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=AAW12_07480 {ECO:0000313|EMBL:KKO91983.1};
OS   Sphingobacterium sp. Ag1.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=1643451 {ECO:0000313|EMBL:KKO91983.1, ECO:0000313|Proteomes:UP000034524};
RN   [1] {ECO:0000313|EMBL:KKO91983.1, ECO:0000313|Proteomes:UP000034524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ag1 {ECO:0000313|EMBL:KKO91983.1,
RC   ECO:0000313|Proteomes:UP000034524};
RA   Pei D., Yu W., Kukutla P., Xu J.;
RT   "Draft Genome Sequences of Sphingobacterium sp. Ag1 from Mosquito Anopheles
RT   gambiae.";
RL   Submitted (APR-2015) 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:KKO91983.1}.
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DR   EMBL; LBGU01000031; KKO91983.1; -; Genomic_DNA.
DR   RefSeq; WP_046672985.1; NZ_LBGU01000031.1.
DR   AlphaFoldDB; A0A0M2XWI6; -.
DR   PATRIC; fig|1643451.3.peg.2620; -.
DR   Proteomes; UP000034524; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 2.
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; PF13426; PAS_9; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 1.
DR   SMART; SM00091; PAS; 2.
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); 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:KKO91983.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000313|EMBL:KKO91983.1}.
FT   DOMAIN          10..83
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          86..138
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          288..503
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   509 AA;  57888 MW;  1B0EDF842A52BBE8 CRC64;
     MGKRASGIND LNIYLKALNS AYSGIIITDN LQDDNPIIYC NKAFENISGY SHDEIIGHNC
     RFLQAQDRSQ PERNILKDSI KNGEECKIEI RNYRKDGTLF WNELFISPVK NEAGQVTHFI
     GVQNDITLRK RAEHELREEK NNVEIKIQQR TKELQDKESF LSSMIETVRE SLLVLDGNYT
     VLSANKHFLT SFHVSSEETV GKLLFDLGNK QWNISSLKEL LTHILPTSNP VIDYEVEHVF
     PHIGRKVMLL NAYRVEFEGQ YKDRILIAIE DITEKKEQDL RKDDFLSVAS HELKTPLTTI
     KGLVQILQRL SIDHSDSKFV STLDKISAYI DRLNILITKL LDTSKIQSGN IELHMEPFNI
     DHTIREAIDN MTLGAPGYEI NLSGFTEATV SGDELQIIQV INNLLSNAIK YSPGSNRIDV
     AIHRVANFVK VSVRDYGMGI ADVDKQKIFE RFFRAGHTQK KFPGLGIGLY VSHEIITHHN
     GTLWVESEPG EGSTFNFTLP IMRTESDGK
//
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