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Database: UniProt
Entry: A6ULF2_SINMW
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Original site: A6ULF2_SINMW 
ID   A6ULF2_SINMW            Unreviewed;      1160 AA.
AC   A6ULF2;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=Blue-light-activated histidine kinase {ECO:0000256|ARBA:ARBA00021740};
DE            EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Smed_5776 {ECO:0000313|EMBL:ABR64482.1};
OS   Sinorhizobium medicae (strain WSM419) (Ensifer medicae).
OG   Plasmid pSMED02 {ECO:0000313|EMBL:ABR64482.1,
OG   ECO:0000313|Proteomes:UP000001108}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=366394 {ECO:0000313|EMBL:ABR64482.1, ECO:0000313|Proteomes:UP000001108};
RN   [1] {ECO:0000313|Proteomes:UP000001108}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM419 {ECO:0000313|Proteomes:UP000001108};
RC   PLASMID=Plasmid pSMED02 {ECO:0000313|Proteomes:UP000001108};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G.,
RA   Richardson P.;
RT   "Complete sequence of Sinorhizobium medicae WSM419 plasmid pSMED02.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABR64482.1, ECO:0000313|Proteomes:UP000001108}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM419 {ECO:0000313|EMBL:ABR64482.1,
RC   ECO:0000313|Proteomes:UP000001108};
RC   PLASMID=Plasmid pSMED02 {ECO:0000313|Proteomes:UP000001108};
RX   PubMed=21304680; DOI=10.4056/sigs.43526;
RA   Reeve W., Chain P., O'Hara G., Ardley J., Nandesena K., Brau L., Tiwari R.,
RA   Malfatti S., Kiss H., Lapidus A., Copeland A., Nolan M., Land M.,
RA   Hauser L., Chang Y.J., Ivanova N., Mavromatis K., Markowitz V.,
RA   Kyrpides N., Gollagher M., Yates R., Dilworth M., Howieson J.;
RT   "Complete genome sequence of the Medicago microsymbiont Ensifer
RT   (Sinorhizobium) medicae strain WSM419.";
RL   Stand. Genomic Sci. 2:77-86(2010).
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L-
CC         glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:24452, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:10311,
CC         ChEBI:CHEBI:29973, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:82795; EC=2.1.1.80;
CC         Evidence={ECO:0000256|ARBA:ARBA00001541};
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DR   EMBL; CP000740; ABR64482.1; -; Genomic_DNA.
DR   RefSeq; WP_011970590.1; NC_009621.1.
DR   RefSeq; YP_001314415.1; NC_009621.1.
DR   AlphaFoldDB; A6ULF2; -.
DR   GeneID; 61614152; -.
DR   KEGG; smd:Smed_5776; -.
DR   PATRIC; fig|366394.8.peg.2284; -.
DR   eggNOG; COG1352; Bacteria.
DR   eggNOG; COG2201; Bacteria.
DR   eggNOG; COG2433; Bacteria.
DR   eggNOG; COG3920; Bacteria.
DR   HOGENOM; CLU_000892_0_1_5; -.
DR   OrthoDB; 9816309at2; -.
DR   Proteomes; UP000001108; Plasmid pSMED02.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR   GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:InterPro.
DR   GO; GO:0008983; F:protein-glutamate O-methyltransferase activity; IEA:RHEA.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd16434; CheB-CheR_fusion; 1.
DR   CDD; cd00130; PAS; 2.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 1.10.155.10; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 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; 2.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR035909; CheB_C.
DR   InterPro; IPR022642; CheR_C.
DR   InterPro; IPR000780; CheR_MeTrfase.
DR   InterPro; IPR022641; CheR_N.
DR   InterPro; IPR036804; CheR_N_sf.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR011102; Sig_transdc_His_kinase_HWE.
DR   InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR   NCBIfam; TIGR00229; sensory_box; 1.
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; PF07536; HWE_HK; 1.
DR   Pfam; PF13596; PAS_10; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   PRINTS; PR00996; CHERMTFRASE.
DR   SMART; SM00911; HWE_HK; 1.
DR   SMART; SM00138; MeTrc; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 3.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF47757; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR   SUPFAM; SSF52738; Methylesterase CheB, C-terminal domain; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS50122; CHEB; 1.
DR   PROSITE; PS50123; CHER; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chemotaxis {ECO:0000256|PROSITE-ProRule:PRU00050};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   FMN {ECO:0000256|ARBA:ARBA00022643};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00050};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Plasmid {ECO:0000313|EMBL:ABR64482.1};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          3..191
FT                   /note="CheB-type methylesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50122"
FT   DOMAIN          204..446
FT                   /note="CheR-type methyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50123"
FT   DOMAIN          788..838
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          842..887
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   COILED          631..725
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        15
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        42
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        133
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ   SEQUENCE   1160 AA;  130614 MW;  036D6FBE6AF80FE5 CRC64;
     MVQKADPPIV AIGASAGGVQ ALQTFFDLMP IDTGATFVVI VHLDPHARSE LANILAARTR
     MPVTQVEDQA RLESNHVYVI APNRRLKIAD GTIAALPFEE PHALRAPIDF FFRSLAEEHR
     SEFAIILTGA GADGAIGVKA IKEADGIVLV QDPDEAEYAS MPRNAIATEV ADFVLPIREL
     PHRVAELLAR RDQLPSHQFR VNDDEMIGRI VAHVRGRTGH DFSQYKRATI LRRIGRRAQV
     ARRETFADYY NYLRENPEEA QALFSDFLIS VTTFFRDPSA FEVLAERVIP HLFDGKEVAD
     KIRVWVPGCA TGEEAYTIGI LLLEEAARRD LSPEIQVFGS DLDEQALRIA REGRYPSTVE
     GDLSEERLRR FFQREGDHYR VRRDLRDAVL FASHSLLRDP PFSHLDMISC RNLLIYLDRQ
     LQQQVCNTFH YALNAGGFLF LGSSESADCP GLFRPVDREA RIYRALAGAG ARPMVLPALL
     GPHKPEMKST IIRTPPAGHG SDAAVHRQML EKIAPPSMLV DESHHAIHLS ENAGRFLKPS
     GGPVSTAATD LVREEFRFDL RAALHRAFGR NEPTLSMPIL ADLDGQPHRV YLQVKPVVRG
     TERTRHALVL FIEGEAIDKT QEVVLDTLDG RPTIDEAIRR LQEELQLAQN RLRLTSEESD
     TATEELRAAN EELQSMNEEY RSTAEELETS KEELQSINEE LQTVNNELKL KLESISRANS
     DLQNLMAATD IATLFLDPSL RIKRFTPRLT EIFNVTSNDE GRPITDFTHR LQYKRLSDDA
     RAVLETLKPV EHEVKGRNDG WYLVRMRPYR TIEDKIDGVV VTFVDISERR HAEEAAKESG
     QRLEQEMRLV ELSRSPIFVW DFDDGVMQWN RGSEELYGYS REEALGRRKE ELLKTGVPGS
     SFDKLRRTLS QKGRWSGELN HTTKDGRVLT VESQIELVPF GERRLVLEST RDITDRKRWE
     RRGQLLLNEL SHRVKNTLAV VQSLARQTLR TTRSSEDFVE RFEGRLAALA SAHKLLVDSE
     WSGAELNELA RRQLDAYAAS DRRRLQIEGE PVTLPPDLAT PFGLVLHELA TNAAKYGAFS
     TGNGQIKLSW KLGNNGRSLG VIWQERGGPP VEPPSEQGFG GVLIEKSLPG STVHRDFQPD
     GVVCTIDIEL PEIRPDGGEK
//
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