ID A0A1F1Q723_9PSED Unreviewed; 1376 AA.
AC A0A1F1Q723;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Chemotaxis protein {ECO:0000313|EMBL:OFS73062.1};
GN ORFNames=HMPREF3173_13585 {ECO:0000313|EMBL:OFS73062.1};
OS Pseudomonas sp. HMSC08G10.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1581141 {ECO:0000313|EMBL:OFS73062.1, ECO:0000313|Proteomes:UP000179079};
RN [1] {ECO:0000313|EMBL:OFS73062.1, ECO:0000313|Proteomes:UP000179079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMSC08G10 {ECO:0000313|EMBL:OFS73062.1,
RC ECO:0000313|Proteomes:UP000179079};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-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 -!- 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:OFS73062.1}.
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DR EMBL; LWMZ01000052; OFS73062.1; -; Genomic_DNA.
DR RefSeq; WP_070573821.1; NZ_KV793307.1.
DR OrthoDB; 9816309at2; -.
DR Proteomes; UP000179079; 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: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 GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd16434; CheB-CheR_fusion; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17580; REC_2_DhkD-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 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; 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; IPR000014; PAS.
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 NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 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; PF13426; PAS_9; 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; SM00091; PAS; 3.
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); 2.
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; PS50112; PAS; 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 Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 26..204
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 228..483
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 869..924
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1012..1233
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1255..1371
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 668..734
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 32
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 59
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 151
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT MOD_RES 1304
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1376 AA; 152702 MW; 876132BA429B7A90 CRC64;
MKSSSKPAVA SPQNPTLSPS HLDFPVVGIG ASAGGLEAIC TFFKQMPADC DMAFVVVLHL
SADHQSVADR IIQETTAMPV RQVSEPVPIE RNHVYVISPA NRLSTNDGYL RVSPANRRRG
DHVAIDLFFR DLADVHKDHA FCVVLSGTGA DGAVGLSRIK EQGGVTLVQS PDDALYDSMP
RAALETGMVD AVLPVAEMPQ KLMELWRNAR QVRLPTIEDD TLPPALGTRS GDPAQAEPLL
DEILLLLRTN TGHDFQHYKR ATVLRRIERR LHVTGQPNLA AYQRYLEQHP AESAELLADM
LIGVTNFFRD REAFESLERH VLPELVSDGE SGEGPSEVRV WSAGCSTGEE AYSLAMLVCE
QLALERRAAK VQVFATDLDE RAIGTARTGL YPESIVTDVP PARLRQFFIK EDQHYRVRKE
IREKVLFARH NLLSDPPFSQ IDLIVCRNLL IYLDREVQRD ILQMFHFALR PGGHLFLGTS
ESVDVASELF IPVDKRNRIF RASPASPAIR SSGRLLPGAE VSAALQDSQA KLRPGRKLSY
AEVHHRALAK RTPPSLILDG DGNILHMSDG VGRFLHLVGG EPSRNLINLV LPQLRLALRS
TLFQARQGNE AVTSRPVELG QMQVEIAVHP HKDEPSGSEC LLVVFEERVP DPSLLPTSAI
RQTDSMVLNN LERELQRTRL QLQETIEQSE ISSEELTASN EEMQAINEEL RSASEELETS
KEELQSINEE LLTVNYELKN KVEETDKVND YLSNLIASTA IATVFVDRNL RIRWFTPRAA
DIFNILSVDT GRSLLDITHR LDYPELADDA RAVAQGTPSI EREVCGENQH WYLARLLPYR
ANEQKIDGTV LTFIDISKGR AAEERLRLGE ERMRLVAEST HDFAIILLDE HGVITDWNTG
ATLIFGHTKD EVVGRHYELI FTEEDRANSV PSRELRGARL NGRGQDERWH VRKDGSRFFC
SGEVSLLKGS SLLGYVKIAR DLTGHKRLHD EQSKQLAESQ SSSHMKDEFF AIMSHELKHP
LNLIQLNAEI LRRLPSVKNT GAASKAVGTI CEAVASQARI IDDLLDVARI RTGKLKLKTE
PVNLCTILRD IHAVVRSEQH PCDVVLELPA DDNALFIEGD ITRLEQIIWN LLNNALKFSP
AGSEIRLVLS SHGEQAQLQV IDQGLGLSEE SLENIFDLFT QAAPQVTSHS REGLGIGLSL
VRQLAQAHGG SVQASSPGLG KGCTFTVRLP LCHFSPQLQH SPGDQQMAPR LDNTRVLLVD
DSPDVLEIMQ QLLEMEGAQV HAFTDPRAAL KAAANGQYDI ILSDIGMPVM DGHALIKALR
EHPHLHDIPA IALTGYGASA DQYKSRQSGF DRHLNKPVAY DELVEAIEAL SGSQPY
//