ID A0A177MWK4_9GAMM Unreviewed; 873 AA.
AC A0A177MWK4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Chemotaxis protein CheB {ECO:0000313|EMBL:OAI10107.1};
GN ORFNames=A1359_02125 {ECO:0000313|EMBL:OAI10107.1};
OS Methylomonas lenta.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylomonas.
OX NCBI_TaxID=980561 {ECO:0000313|EMBL:OAI10107.1, ECO:0000313|Proteomes:UP000078476};
RN [1] {ECO:0000313|EMBL:OAI10107.1, ECO:0000313|Proteomes:UP000078476}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R-45370 {ECO:0000313|EMBL:OAI10107.1,
RC ECO:0000313|Proteomes:UP000078476};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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:OAI10107.1}.
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DR EMBL; LUUI01000160; OAI10107.1; -; Genomic_DNA.
DR RefSeq; WP_066987708.1; NZ_LUUI01000160.1.
DR AlphaFoldDB; A0A177MWK4; -.
DR STRING; 980561.A1359_02125; -.
DR OrthoDB; 9816309at2; -.
DR Proteomes; UP000078476; 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: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; cd16434; CheB-CheR_fusion; 1.
DR CDD; cd00130; PAS; 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; 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 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; PF13596; PAS_10; 1.
DR PRINTS; PR00996; CHERMTFRASE.
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); 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF57997; Tropomyosin; 1.
DR PROSITE; PS50122; CHEB; 1.
DR PROSITE; PS50123; CHER; 1.
PE 4: Predicted;
KW Chemotaxis {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Reference proteome {ECO:0000313|Proteomes:UP000078476}.
FT DOMAIN 25..215
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 234..480
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 38
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 65
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 157
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 873 AA; 98443 MW; 4D7A3DD514864766 CRC64;
MPISKTQTPD TLITQKSTKK PPRNRASGIP RIVGIGASAG GLEALEAFLS HMPADSGLAF
VIIQHLDPVH KGVMPELLQR ITPMRVTQAG NRMKVKANCV YVIPPNKDLS VLHGSLYLLD
PVAARGLRLS IDFFFRSLAE DQHERAIGVI LSGMGSDGTL GLRAIKENAG LSLVQDPETA
KFDAMPRSVI QAGLADIVAP AQELPTHIIN YLNHSHHVAD SSIVGSEPIL PLKSQNSLEQ
IIILLRERTS HDFSLYKKNT IYRRIERRMG LHKIDAIASY VRYLRENPHE LDLLFKELLI
GVTNFFRDPA VWEQLKTVAL PALLDNYLMG KPLRAWVPAC STGEEAYSLA MVFNEVLNQR
QSQTGFSLQI FATDLDDDAI EKARQGFYRA NISEDVSTER LKRFFIQEEN GYRISKTIRE
MVIFAPQNII MDPPFTKLDI ISCRNLMIYL DQQLQNKLIP LFHYALTAHG LLMLGNAETI
GSQISLFKPI DKNARLYQRI DNILPMTSSL EFPIKYFPVS VLAEKEPRST QSMTGQPANL
ETLTEQFLLR HFTPAAVLVN TDGDIVYISG RTGKYLEPAA GKANWNIYAM AREGLRNELA
LALKKAQRQP EAVFVPDLTL DMNGIPHSIN LTVQALTSPD LLCNKLIVVF NDIAPPLSGK
LRRRKPGAIQ KLLETQLQQA LEDLQTTREE MQSSQEELKS ANEELQSSNE ELQSTNEELN
TSKEEMQSLN EELQTVNAEL QSKVEDLTWV NNDMKNLLDS MEIATVFLDN QLKIRRFTSY
ATHLFKLIPG DLGRQLSDIV TDLDYPQFMA DIQKVAQTLA FIDQQIKTFD NRWFKVRIMP
YRTQDNVIDG VVITFVDICE IKQLEAELRD KIE
//
