ID H1Y749_9SPHI Unreviewed; 1605 AA.
AC H1Y749;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE SubName: Full=Signal transduction histidine kinase with CheB and CheR activity {ECO:0000313|EMBL:EHQ28668.1};
GN ORFNames=Mucpa_4579 {ECO:0000313|EMBL:EHQ28668.1};
OS Mucilaginibacter paludis DSM 18603.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=714943 {ECO:0000313|EMBL:EHQ28668.1, ECO:0000313|Proteomes:UP000002774};
RN [1] {ECO:0000313|EMBL:EHQ28668.1, ECO:0000313|Proteomes:UP000002774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18603 {ECO:0000313|EMBL:EHQ28668.1,
RC ECO:0000313|Proteomes:UP000002774};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Held B.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The permanent draft genome of Mucilaginibacter paludis DSM 18603.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CM001403; EHQ28668.1; -; Genomic_DNA.
DR RefSeq; WP_008509545.1; NZ_CM001403.1.
DR STRING; 714943.Mucpa_4579; -.
DR eggNOG; COG1352; Bacteria.
DR eggNOG; COG2201; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000892_2_1_10; -.
DR OrthoDB; 9813151at2; -.
DR Proteomes; UP000002774; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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 CDD; cd16434; CheB-CheR_fusion; 1.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 1.10.287.130; -; 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; 5.
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; 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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR24422; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR PANTHER; PTHR24422:SF25; CONSERVED HYPOTHETICAL CHEMOTAXIS PROTEIN; 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; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00996; CHERMTFRASE.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00138; MeTrc; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 4.
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; 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); 5.
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; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Chemotaxis {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Kinase {ECO:0000313|EMBL:EHQ28668.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002774};
KW Transferase {ECO:0000313|EMBL:EHQ28668.1}.
FT DOMAIN 13..202
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 205..455
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 993..1065
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1069..1121
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1122..1194
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1197..1247
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1389..1605
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 649..718
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 955..982
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 25
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 52
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 144
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 1605 AA; 182503 MW; 0D47A43C12061C8F CRC64;
MAKVKPLQFP ESKLADRYII AIGASAGGLE AIHDFFDHMP GNSGFTFVVI QHLSPDYKSL
LVDLVSKHTH MKVFEATNDV ILQRDCVYII PNKKIMTIRG NKLRLVDKIK DKSPNTAIDT
FLFTLAKDKK DKAIAIILSG TGTDGTKGVE AIKECGGMVI VQDPATAKFD GMPNSAITSG
NADFILPPAK MHVEVYNYVN QRHLPLLEQD QLDDNLLNEI FRLVHISSGQ DFNLYKTPTI
LRRIARRMAA VEIDRLENYI GLLHQDPQEV KVLAKDFLIG VTKFFRDKPA FDILAQQIIP
AIVKSKQEGE IIKIWVCACS TGEEAYSIAI LFNDYLDRTG ESRELKIFAT DVDESSIEIA
ARNCYPLSIG NEVPAALLSK YFVKDDKNYS VLPGIRKQIV FARHNVIKSP PFIKNDLVTC
RNMLIYMNNL LQQKIMSTFH YALNKEGYLF LGSSENAASI KEGVNEISGK WKIYQKTGTI
NYGLHHTYTT ATPNLKYTEK RPLAKPGEYQ KHMEEEFREL MISEFSAVGI FIDKSYIIKE
TIGNYSRYLN LPEKKLDLNI LNMVNREVSV MLNTAIRKAW KERQKTHLNR VKLKHDDREQ
LLQITVKPPD ESSTNDYTLL LFSEIKTDPV SKEGIVLPPV NAGSDQEYLM EMEAELSETR
INLQMAVEEM ETTNEELQSS NEELLSANEE LQSGNEELQS LNEELHTLNT EHQLKIRELV
ELNDDLDNYF RSTDIGQIFV DANLRIRKFN PAAINMINLI DADVGRPINH LSNNILYDNL
IADIHSVLAT GQVIEKEVLL KSGTNNLMRI MPYVKKDGQH DGVVISFIDI SVIVELNQII
SGVFNASTAA ILAFRDNRTE GSKNPDFRCI AYNDAALTLF GKPAVEMDAQ PRLQSFPELI
GIASAEQYAK AARQSKAWET ELHTGQDNWY QVTIGPMREG FVVSLTNITA RKNAEQKLKK
NYHELINARE GLKNLNSQLE NKVYERTQKL TESEERFKLV STATNDTIWD WNLVSNTMWR
SDNFTSMFGY QRDDETNQIS FWFGKIHPDD RLRVEQSVFN AINHHEKQWS AEYRFQKADG
TYAIILDRGR ILEDEFHTPY RLVGSIIDIT RLIETEKRLS QSENKFRKVF DSNLIGMCFA
DPDGRLLETN DAFLNMLGYS RADMETGQLN LQNLTPPTSR QASSRAQKEL DENGFCQPYE
KQYIRKDGSL VSVLKGSAML SEDEKQISVS YILDITRQKE LQHMISKQQE EFYSIFTNAP
ALITIRRGPN LVYEFVNNAF IRLDGQQNYI GRSTAEINQW WPGTELGRAD AEVMRSGQPF
TGRSVRIQWP NAQTGKQADH WFDFIFTPVF NDDDKLDGIA FFGFDVTELV KARETTEELM
HKKDEFLSIA SHELKTPITS LKGSLQILQR IMAREGGKNT VMDFVGKANN QTNKLTTLVD
DLLDVTKIQA GKLLLNYETF DAVQLVKEVL EEVRAQEGTH EFILQGEGLI TITADRTRLE
QVITNFLTNA IKYSPKGDKV ILNCSLFENE FKLTVQDFGI GIPEAKKDYL FDRFYRVQES
STHFSGLGLG LYISAEIIKR HRGQIGVESA IGEGATFWFT VPLQP
//