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Database: UniProt
Entry: D5RM09_9PROT
LinkDB: D5RM09_9PROT
Original site: D5RM09_9PROT 
ID   D5RM09_9PROT            Unreviewed;       672 AA.
AC   D5RM09;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=cheA5 {ECO:0000313|EMBL:EFH11660.1};
GN   ORFNames=HMPREF0731_2120 {ECO:0000313|EMBL:EFH11660.1};
OS   Pseudoroseomonas cervicalis ATCC 49957.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Pseudoroseomonas.
OX   NCBI_TaxID=525371 {ECO:0000313|EMBL:EFH11660.1, ECO:0000313|Proteomes:UP000005324};
RN   [1] {ECO:0000313|EMBL:EFH11660.1, ECO:0000313|Proteomes:UP000005324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49957 {ECO:0000313|EMBL:EFH11660.1,
RC   ECO:0000313|Proteomes:UP000005324};
RA   Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA   Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA   Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA   Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA   Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA   Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA   Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA   Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA   Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA   Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL   Submitted (APR-2010) 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   -!- 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:EFH11660.1}.
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DR   EMBL; ADVL01000341; EFH11660.1; -; Genomic_DNA.
DR   RefSeq; WP_007004537.1; NZ_GG770779.1.
DR   AlphaFoldDB; D5RM09; -.
DR   HOGENOM; CLU_000650_5_0_5; -.
DR   Proteomes; UP000005324; 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; cd00731; CheA_reg; 1.
DR   CDD; cd16916; HATPase_CheA-like; 1.
DR   Gene3D; 3.40.50.2300; -; 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; 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; IPR011006; CheY-like_superfamily.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43395:SF10; CHEMOTAXIS PROTEIN CHEA; 1.
DR   PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR   Pfam; PF01584; CheW; 2.
DR   Pfam; PF02895; H-kinase_dim; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00260; CheW; 2.
DR   SMART; SM01231; H-kinase_dim; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF50341; CheW-like; 2.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50851; CHEW; 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005324};
KW   Transferase {ECO:0000313|EMBL:EFH11660.1}.
FT   DOMAIN          9..249
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          251..389
FT                   /note="CheW-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50851"
FT   DOMAIN          408..537
FT                   /note="CheW-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50851"
FT   DOMAIN          549..666
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         599
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   672 AA;  70923 MW;  DCC7E0C7C290C4BF CRC64;
     MQAIRVSLTV LDELMTLASE LVLVRNQLLQ VARGQADTPF AAPLQRLSRI TSDLQEGVMK
     TRMQPVSAAW AKLPRLVRDL GAELGKRIDL SMSGGDTELD RQVLELIKDP LTHMVRNSAD
     HGLEMPEERR AAGKPLAGRI SLSARQEGGR IVIELADDGR GLNLAKIRVR AVERGLATEA
     AVAAMDDAEV GRFIFRPGFS TAAAVTAVSG RGVGMDVVRS NIERIGGTVD LQTVEGQGTT
     LIIRIPLTLA IISGLVVQAA GERFAVPQAA VVELVRVGSG GAAVEWLDDA PVIRLRGQLL
     PLVQLGALLG LAAPHPSGSA AQGFVAVLQG DSARYGLFVD GVFDTEEIVV KPVAPILRDL
     QAFSGNTILG DGGVIMILDP AGLARMAGLG TARKEAAQAV ATASEETGSQ LLMFRAGGQA
     TPIAVPLGLV ARLEALPSDS IEIAGNRPSV QYRGQLMPLL PLGPWTQPPA GGTQHLLVFQ
     DGNRSLGLMV DEILDVIEER LVLRPSSDRA GFLGSAVVAG RAADVLDCAH WLRLGDPSWF
     GKTEQAAPRV LVVEDSGFFR QLVVPALTSA GYDVTACAEP AEALKLRAGG AMFDVVLSDI
     EMPNMDGFGF VAEIRREGPW QTLPVVALSS RSSPADIARG RAAGFTDHVA KFDSERVLGA
     LSRALAHAKE AA
//
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