ID A0A011UDW3_RUMAL Unreviewed; 808 AA.
AC A0A011UDW3;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=RASY3_10735 {ECO:0000313|EMBL:EXM38824.1}, RASY3_19425
GN {ECO:0000313|EMBL:EXM38353.1};
OS Ruminococcus albus SY3.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=1341156 {ECO:0000313|EMBL:EXM38824.1, ECO:0000313|Proteomes:UP000021369};
RN [1] {ECO:0000313|EMBL:EXM38824.1, ECO:0000313|Proteomes:UP000021369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY3 {ECO:0000313|EMBL:EXM38824.1,
RC ECO:0000313|Proteomes:UP000021369};
RA Dassa B., Borovok I., Lamed R., Flint H., Yeoman C.J., White B.,
RA Bayer E.A.;
RT "Rumen cellulosomics: divergent fiber-degrading strategies revealed by
RT comparative genome-wide analysis of six Ruminococcal strains.";
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:EXM38824.1}.
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DR EMBL; JEOB01000004; EXM38353.1; -; Genomic_DNA.
DR EMBL; JEOB01000003; EXM38824.1; -; Genomic_DNA.
DR RefSeq; WP_037288029.1; NZ_JEOB01000004.1.
DR AlphaFoldDB; A0A011UDW3; -.
DR PATRIC; fig|1341156.4.peg.2091; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000021369; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 1.10.287.560; Histidine kinase CheA-like, homodimeric domain; 1.
DR Gene3D; 3.30.70.1110; Histidine kinase CheA-like, P2 response regulator-binding domain; 2.
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; IPR037052; CheA-like_P2_sf.
DR InterPro; IPR010808; CheA_P2-bd.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
DR InterPro; IPR035891; CheY-binding_CheA.
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 Pfam; PF07194; P2; 2.
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; SSF55052; CheY-binding domain of CheA; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000021369};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 4..114
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 425..661
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 663..802
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 360..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 55
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 808 AA; 88430 MW; A870E6664C8B8626 CRC64;
MPKFDESMES MVDTFLFETG ELLENLDEIL MRAEQAEEIS MIEESDIAEI FRTMHTIKGS
AAMMGLQNMS TLAHAMEDMF FIIREKTYVR TDKAALFDLL YKSSDALKAE LENLTDEDIP
LTDFSEMIGH IHDLAAFFKG EGGNTEEQSD DVPADIFDDN EPADMLTYKL IYDDACQMPS
ARAIVLIRKL GAFAEVCRTI PPDMDDDNAD GQIKNAGLYI KLVTDDRNAV EKMISAALNV
ENFELFTRDK LKAKSGGEKG GNNEISIPEG VFLPDDGDEL LTYRVTYSES CAMPSARAIV
LLRKLGAVSE VCRTLPPDMD ADDADDAIKK NGLYIKLITD DTAAVEKMLQ SGINVESAVK
VDKSDAVKEA PKAGTAEKAE AQKTENKAET QAEQSPKPAA KAQKKEHKEQ SMLTVKLEKL
DKLLELVSEI VITESAVTSS PDLRELDTNL DRFNKSSREL KKLTDELQDV VMSLRMVPVS
TAFQKMNRVV RDMNNTLKKN ANLVFRGEDT EVDKSIIDML GDPLMHIVRN AVDHGIETPE
ERAASGKKNP PTVTLSAGYE SNEVVISCKD NGAGMDAAKI MAKAKKNGLL TKPESEYTER
EIFNFVVAAG FSTNETVTQY SGRGVGMDVV KQNIEKVGGK LTVNSKLGKG STFTIRIPLS
LSIVDVLSVE IGSSSISIPA LSVREAFSCT AENVITDPDG NEFVYLRDKC LPLIRLGEKL
QLNTDITDPT EGICIYCREG AYEAVLLADS IVCDQQVVVK PFSPLLDGLH LKEAGLAGCS
ILGDGSITII LDMLSLLGGE KGEETSNG
//
