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Database: UniProt
Entry: A0A177QVB4_9PROT
LinkDB: A0A177QVB4_9PROT
Original site: A0A177QVB4_9PROT 
ID   A0A177QVB4_9PROT        Unreviewed;       706 AA.
AC   A0A177QVB4;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, 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=AYO46_10020 {ECO:0000313|EMBL:OAI50493.1};
OS   Betaproteobacteria bacterium SCGC AG-212-J23.
OC   Bacteria; Pseudomonadota; Betaproteobacteria.
OX   NCBI_TaxID=1799662 {ECO:0000313|EMBL:OAI50493.1, ECO:0000313|Proteomes:UP000077532};
RN   [1] {ECO:0000313|Proteomes:UP000077532}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCGC AG-212-J23 {ECO:0000313|Proteomes:UP000077532};
RA   Choi J., Stepanauskas R., Howe A.;
RL   Submitted (FEB-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   -!- 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:OAI50493.1}.
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DR   EMBL; LSTF01000094; OAI50493.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A177QVB4; -.
DR   Proteomes; UP000077532; 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; cd16934; HATPase_RsbT-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00156; REC; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 2.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF13581; HATPase_c_2; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 2.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 2.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 2.
DR   SUPFAM; SSF52172; CheY-like; 2.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000077532}.
FT   DOMAIN          225..445
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          467..580
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          583..698
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          160..208
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         516
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         632
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   706 AA;  76795 MW;  FFE8B338A2F9189D CRC64;
     MTIRLLTVAV RQEQDVVSAR QRARQVARLL GFEGQDQARI ATAVSEIVRN AFRYAGGGEV
     EFSIEGERAP QLLAVHVKDQ GGGIPHLQTV LDGKYRSATG MGLGIVGARR LMDHFTIRPT
     AKGTTVTLQK LLPQQAALIT QAQAGQIAAA LAKEGAASPV DEVQQQNREL MRTLQDVRER
     QEELQGVNRE LEDTNRGVVA LYAELEERAD YLRRADETKS RFLSNMSHEF RTPLNSIRAL
     TQILLDRADG PLSSEQEVQL NFIRGAAQNL SELVDDLLDI AKIEAGKIDV RPTQFSVQDL
     FSALRGMLRP LLVGDKVALR FDAADDLPPL LSDEGKLSQI LRNLISNALK FTERGEIRVS
     AYLAEDRARI EFAVADTGIG IAPEDHDRIF EEFVQVRNPL QGRVKGTGLG LPLCRRLATV
     LGGTITLEST PGAGSVFSVR LPLRAPAAAP DLALAPEQLA IAPGLIPVLV VEDQPGEQVI
     YAKMLEGTAY GPIPAHNLRQ AREGLAQGKP AAVLLDIQLG YETTWKWLGE VKSDPATAAL
     PIIVVTSVED PRKSAALGAD AYLDKPVSRV ALLDALNELT RARVLIIDDD PASRYTIRKC
     FQDQPYQILE AANAREGMRT AAAMRPEFIV LDLNLPDRRG EEVLDELAGG EGTRSIPVLI
     ATSESLTPAL RERLGGAAAV LSKADLNRES LSRVLASIRE RAVPPA
//
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