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Database: UniProt
Entry: A0A1F1Q723_9PSED
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Original site: A0A1F1Q723_9PSED 
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
//
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