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Database: UniProt
Entry: A0A371BEW6_9SPHN
LinkDB: A0A371BEW6_9SPHN
Original site: A0A371BEW6_9SPHN 
ID   A0A371BEW6_9SPHN        Unreviewed;      1202 AA.
AC   A0A371BEW6;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=DXH95_01405 {ECO:0000313|EMBL:RDV06124.1};
OS   Sphingorhabdus pulchriflava.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingorhabdus.
OX   NCBI_TaxID=2292257 {ECO:0000313|EMBL:RDV06124.1, ECO:0000313|Proteomes:UP000263833};
RN   [1] {ECO:0000313|Proteomes:UP000263833}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GY_G {ECO:0000313|Proteomes:UP000263833};
RA   Kim S.-J., Jung G.-Y.;
RL   Submitted (AUG-2018) 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:RDV06124.1}.
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DR   EMBL; QRGP01000001; RDV06124.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A371BEW6; -.
DR   OrthoDB; 9816309at2; -.
DR   Proteomes; UP000263833; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   CDD; cd16434; CheB-CheR_fusion; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00156; REC; 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; 3.40.50.180; Methylesterase CheB, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR035909; CheB_C.
DR   InterPro; IPR022642; CheR_C.
DR   InterPro; IPR000780; CheR_MeTrfase.
DR   InterPro; IPR022641; CheR_N.
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; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR24422; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR24422:SF25; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR   Pfam; PF01339; CheB_methylest; 1.
DR   Pfam; PF01739; CheR; 1.
DR   Pfam; PF03705; CheR_N; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF13596; PAS_10; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00996; CHERMTFRASE.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00138; MeTrc; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF47757; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF52738; Methylesterase CheB, C-terminal domain; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS50122; CHEB; 1.
DR   PROSITE; PS50123; CHER; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Chemotaxis {ECO:0000256|ARBA:ARBA00022500, ECO:0000256|PROSITE-
KW   ProRule:PRU00050}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00050};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000263833}.
FT   DOMAIN          7..188
FT                   /note="CheB-type methylesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50122"
FT   DOMAIN          208..455
FT                   /note="CheR-type methyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50123"
FT   DOMAIN          846..1059
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1082..1199
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          622..716
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        18
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        45
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        137
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT   MOD_RES         1133
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1202 AA;  132024 MW;  273E5818F9E682DF CRC64;
     MPDMQYPVEF PVVGVGASAG GLEAFSGLLE AISDTSGKAF IFVQHLDPKH ESLLVDLLGT
     HTSLQIKQAT EGLRVDPNHI YIIPPSAYLA VRKGVLHITR PSSKHGARLP FDFLLKSLAE
     NYGPRAMAVV LSGTGADGSE GISAIKNKGG IVYAQDPSEA EYGGMPECAI DTGCVDATAT
     VAAIGSLLSM RTANPSAQSD QRDAQTAIIE LLRATTPHDF RLYKPGTLQR RIERRMLLAS
     ISPEKMADYL ERLQQDHEER DLLAKDLLIN VTSFFRDPKV FETLGTTFLP DLIAKHPANE
     PLRIWVAGCS TGEEAYSFAI VFREVLTALN SRIKLQVFAS DVDADAVGFA REGIYPATIA
     ADVSPERLAR FFIADGQGYR VTRELRSTVV FSVQDILSDP PFSRLDLVSC RNLLIYLGPE
     AQAKVIAILH FALRNDGILL LGNAETIANV EGRFEILSKD KRIYRHLGRT GLAGVGFHMN
     ADNLLRLPPG IGQRSVGKRH ASLAEFCEQQ VLDRYAPAAV LINRNQECLY TVGPVERYLQ
     IAAGHPTHDL LAMVAPTLRA HLRTALLAVN PASPSVVKPG GKIDSAPFNI EVQSVDYEGE
     ELRLVCFLDA PMRNSKVAPS PVTTESERIN ELEKELQVTR SELQVAINNL EMSVEEQHAV
     NEEALSVNEE FQSTNEELLT SKEELQSLNE ELTALNSQLQ ESLERQRTTS NDLQNVLYST
     DVATLFLDMQ FNIRFFTPAT RALFSIIASD IGRPLSDLNS LASDTALLED ARTVLESLDP
     IDREIQVGGD IWFVRRIMPY RTDNGVEGVV ITFTDISERR HAAKIVDEAK KAAERATVAK
     SRFLAVASHD LRQPLQTLSL LQGLLAKSVE GEKPQRLVAR LDETLGAMTG MINTLLDINQ
     IEAGTITTQI SRFPISDLLD QLRDEFSYHA KAKKLELRVV QCSVVVQTDR RLLEQMLRNL
     LSNALKYTER GRILMGCRRL ADGISIEILD AGIGIAPDQI HAIFDEYHQV DNAARERSRG
     LGLGLSIVQR LGKLLGHPVR VRSVLGKGSA FAVEVKLPLN ELVDGPAPAT ASSKANTFRT
     ANILIVEDDP EVRLLLEQLL SDEGHITATA VDGKASLKLV ESGKMQPDLV LADYNLPKGM
     NGLQLATKLR TMINTELPVI ILTGDILTET MREVAAQNCM QLNKPVKVGE LSKTIQKLLA
     RP
//
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