ID A0A0Q4CSP8_9SPHN Unreviewed; 1148 AA.
AC A0A0Q4CSP8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Chemotaxis protein {ECO:0000313|EMBL:KQM28116.1};
GN ORFNames=ASE58_07365 {ECO:0000313|EMBL:KQM28116.1};
OS Sphingomonas sp. Leaf9.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1735674 {ECO:0000313|EMBL:KQM28116.1, ECO:0000313|Proteomes:UP000051210};
RN [1] {ECO:0000313|EMBL:KQM28116.1, ECO:0000313|Proteomes:UP000051210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf9 {ECO:0000313|EMBL:KQM28116.1,
RC ECO:0000313|Proteomes:UP000051210};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQM28116.1, ECO:0000313|Proteomes:UP000051210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf9 {ECO:0000313|EMBL:KQM28116.1,
RC ECO:0000313|Proteomes:UP000051210};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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 -!- 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};
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:KQM28116.1}.
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DR EMBL; LMKC01000002; KQM28116.1; -; Genomic_DNA.
DR RefSeq; WP_055819246.1; NZ_LMKC01000002.1.
DR AlphaFoldDB; A0A0Q4CSP8; -.
DR Proteomes; UP000051210; Unassembled WGS sequence.
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:InterPro.
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; 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; 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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
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 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; PF08447; PAS_3; 1.
DR PRINTS; PR00996; CHERMTFRASE.
DR SMART; SM00911; HWE_HK; 1.
DR SMART; SM00138; MeTrc; 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.
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 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 S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 16..204
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 208..478
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT REGION 481..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 644..710
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 27
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 54
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 146
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 1148 AA; 125727 MW; 5994EC1B6BE7A0F3 CRC64;
MHDVVSTKAE AMPASPASVP VVGIGASAGG LEALREMLAP AKRPTGLAFV VVQHLDPNHE
SMLAQLLDRN TTLAVLQSSG GERIEADTVY IIPPGRGLAI RDGVLELTDF QQPRGLRRPI
DDFFLSLAGD QQANAACVIL SGTGADGTTG LRAIKENGGV CVVQQPESAR YDGMPLSAVG
TGMIDFVKPP GEILHCLQAF FGRRGSDPIE PEANVVADHV DEMCRVLRTA IGHDFSGYKR
STLVRRVERR MHVLGIDTGR AYLARIRSDA GECEALFRDL LINVTRFFRD ADAFEALRTR
VVEPLMADRP ADEDIRVWVP GCSSGEEAYT IAMLFAEAAR KSGSPLAVQI FATDIDEQML
GIAREGSYPA AAMADVPAHL RERYTVPHAE RFTIAAPIRD MIRFSSHSLV KDPPFSRLDL
VSCRNLLIYF DDRLQQAVLP LFHYALRPGG FLFLGTSESV GRFEHLFLSV DQQARLFERG
PGAPSYPIDL PGSQRQPLPR RERDARGDTT ALGSEALATR RVVERYAPPS LIVDQDGGII
SAYGKLSRYF EFPVTRTGGS SAVNLARPGL RNVIGPLLRQ ARDERRRVIA RDVAVETDYG
TQPVEVICDP LGDGTLLFVF RDTGPFVPSD PGELQDLEPS DDHLESLEDE LRLTRHRLRS
AIEELETANE ELKSSNEEMM SMNEELQSTN EELSTVNDEL KSKVDQLTVA NSDLRNFYES
TELAVVVLDA DLKVRSYTDA ATRIFPLKAT DRGRPLTDVA NRLEDAAHLA DARAVAGGAS
PVQRRVRTSD GEHVFSLRVL PYRTQTGEVD GATLVLTEIT DALALERQLA AERERLDLAI
KAAGIGVWEY CPENGELVLD PAERQLFEVA SDATPRIEDL LGRIDADDLP KVEAALRRVI
ERSGDYESTF RVCRSDGQTR WVKGFGRVVG GSAPQRLVGV SIDVTPEYAL AETRELMLRE
MNHRVKNLFA VIAGMITMAA RSHDDLRTFA DDIRRRIAAL GSAHSLASPA GQPHAVGLDD
IVATTLAPYR DHARIEIDGP VVALDRSCLS PLALILHEWA TNSIKYGALG SDGERGLRVC
WQVGEDGIVL TWTEDAKDTG DLLPGKRGFG SVLVETSVRQ LRGTMTAGMA DGQLRMEVRL
PAGVLLRD
//
