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Entry: A0A0A1YN94_9PSED
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ID   A0A0A1YN94_9PSED        Unreviewed;       618 AA.
AC   A0A0A1YN94;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=TMS3_0101170 {ECO:0000313|EMBL:KFX70581.1};
OS   Pseudomonas taeanensis MS-3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1395571 {ECO:0000313|EMBL:KFX70581.1, ECO:0000313|Proteomes:UP000030063};
RN   [1] {ECO:0000313|EMBL:KFX70581.1, ECO:0000313|Proteomes:UP000030063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS-3 {ECO:0000313|EMBL:KFX70581.1,
RC   ECO:0000313|Proteomes:UP000030063};
RX   PubMed=24407626;
RA   Lee S.Y., Kim S.H., Lee D.G., Shin S., Yun S.H., Choi C.W., Chung Y.H.,
RA   Choi J.S., Kahng H.Y., Kim S.I.;
RT   "Draft Genome Sequence of Petroleum Oil-Degrading Marine Bacterium
RT   Pseudomonas taeanensis Strain MS-3, Isolated from a Crude Oil-Contaminated
RT   Seashore.";
RL   Genome Announc. 2:0-0(2014).
CC   -!- FUNCTION: Involved in the transmission of sensory signals from the
CC       chemoreceptors to the flagellar motors. CheA is autophosphorylated; it
CC       can transfer its phosphate group to either CheB or CheY.
CC       {ECO:0000256|ARBA:ARBA00035100}.
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   -!- 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:KFX70581.1}.
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DR   EMBL; AWSQ01000001; KFX70581.1; -; Genomic_DNA.
DR   RefSeq; WP_025163397.1; NZ_AWSQ01000001.1.
DR   AlphaFoldDB; A0A0A1YN94; -.
DR   STRING; 1395571.TMS3_0101170; -.
DR   eggNOG; COG0643; Bacteria.
DR   OrthoDB; 9803176at2; -.
DR   Proteomes; UP000030063; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR   CDD; cd16916; HATPase_CheA-like; 1.
DR   CDD; cd00088; HPT; 1.
DR   Gene3D; 1.10.287.560; Histidine kinase CheA-like, homodimeric domain; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 1.20.120.160; HPT domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR004105; CheA-like_dim.
DR   InterPro; IPR037006; CheA-like_homodim_sf.
DR   InterPro; IPR036061; CheW-like_dom_sf.
DR   InterPro; IPR002545; CheW-lke_dom.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR036641; HPT_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR   PANTHER; PTHR43395:SF10; CHEMOTAXIS PROTEIN CHEA; 1.
DR   PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR   Pfam; PF01584; CheW; 1.
DR   Pfam; PF02895; H-kinase_dim; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF01627; Hpt; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00260; CheW; 1.
DR   SMART; SM01231; H-kinase_dim; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00073; HPT; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF50341; CheW-like; 1.
DR   SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50851; CHEW; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50894; HPT; 1.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030063};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          1..105
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   DOMAIN          224..474
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          476..612
FT                   /note="CheW-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50851"
FT   REGION          183..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         48
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   618 AA;  67327 MW;  551EF5EDE45321AD CRC64;
     MNFGMNQFLG VFFEEAEEHL TSLENLLLTL DLQEPDPEAL NGIFRAAHSI KGSSGMFGFE
     EMTGVTHVLE TLLDQIRSGQ IRLQVEMIDV FLEARDVLSQ LLDNYRAERP PVDVPVAAVS
     QRLQALIERY SPNNQATPTE QAYGLFDDES PAAADQSEEA YGLFDDEVSQ PAVATEQDDK
     DAAYGFFDTP PQPQGETEPS PTVATQPMAV AKPGPKTTPV GTEAESSSIR VSVERIDSLI
     NQVGELVITQ AMLAQLTSAL DPGEHERIFQ ALNQLDHNTR ELQEAVMSIR MLPISFIFNR
     FPRVVRDTAN KLGKQVELIL RGEHTELDKG VIEKLTDPLT HIVRNSIDHG IETPAERLAA
     GKPERGTVRM SAYHQGGRIV VEVSDDGKGL SRERILAKAK EKGIAVSDDM PDSEVWPLIF
     MPGFSTAETV TDLSGRGVGM DVVRRNITSI GGRIDINSAI GLGTHIAIRL PLTLAILDGM
     IVEVDKVHYV VPLTYIVESL QLKAEHLYSM SGSSSSVISV RNEYLPLLSL HSLLNLATEP
     PPAVGSIVLI LEAEGNTFAL QVDELVGQQQ VVIKSLEQNF RRIDGITGAT IMGDGSVALI
     LDIDALPRLA GQGVANHA
//
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