ID A0A916R8B2_9HYPH Unreviewed; 731 AA.
AC A0A916R8B2;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 28-JAN-2026, entry version 12.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=cheAI {ECO:0000313|EMBL:GGA35713.1};
GN ORFNames=GCM10011499_01300 {ECO:0000313|EMBL:GGA35713.1};
OS Pelagibacterium lentulum.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Hyphomicrobiales; Devosiaceae; Pelagibacterium.
OX NCBI_TaxID=2029865 {ECO:0000313|EMBL:GGA35713.1, ECO:0000313|Proteomes:UP000596977};
RN [1] {ECO:0000313|EMBL:GGA35713.1, ECO:0000313|Proteomes:UP000596977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.15896 {ECO:0000313|EMBL:GGA35713.1,
RC ECO:0000313|Proteomes:UP000596977};
RX PubMed=25193709;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Walter F., Albersmeier A., Kalinowski J., Ruckert C.;
RT "Complete genome sequence of Corynebacterium casei LMG S-19264T (=DSM
RT 44701T), isolated from a smear-ripened cheese.";
RL Int. J. Syst. Evol. Microbiol. 189:76-77(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:GGA35713.1}.
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DR EMBL; BMKB01000001; GGA35713.1; -; Genomic_DNA.
DR RefSeq; WP_127072438.1; NZ_BMKB01000001.1.
DR AlphaFoldDB; A0A916R8B2; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000596977; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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; cd00731; CheA_reg; 1.
DR CDD; cd16916; HATPase_CheA-like; 1.
DR CDD; cd00088; HPT; 1.
DR FunFam; 2.30.30.40:FF:000048; Chemotaxis protein CheA, putative; 1.
DR FunFam; 3.30.565.10:FF:000016; Chemotaxis protein CheA, putative; 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; IPR051315; Bact_Chemotaxis_CheA.
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; IPR036890; HATPase_C_sf.
DR InterPro; IPR003594; HATPase_dom.
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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00110}; Reference proteome {ECO:0000313|Proteomes:UP000596977};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..104
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 378..590
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 592..727
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 320..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..336
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 731 AA; 78937 MW; 2C685BCBB98081D6 CRC64;
MSDLDEFKAT YFDECSELLL ELEEQFIAIQ DGDRSADRLN AVFRAIHSIK GGGGAFGFDG
LVKFAHSFET LLDYVRDGRV ELTEDVITLC IRSIDLVADF VGAARDGITL APDYGATEKA
SFDALARGEA GGSAGSAAGD DLDEFDIDFT PVAVNLDASA PLSAVGSSQE DLTVWQVTFK
PFSSLYERAN DPLLLFRELA LLGDSTVHAE LTQLPSLGQF EPFGVYCTWM IELVSDKANE
EAIREVFEFV DGDCEIGIEK REGVTLAPAV APSDDDDLPS FADLAEQAKA ERKFVPTGEP
DDLESPAPAV AAVKPLTPAR PAVASEAGEE SSTSSGRPAG MQSIRVDLDK VDRVVNMVGE
LVITQSMLTQ QMDDAIRDRY QELVRGVEVL AQTTRGLQDA VMAIRAQPVK SVFSRMPRLV
RELASKTGKK IKLETIGENT EIDKTIIEQL SDPLTHMVRN SADHGVEGIE KRLAAGKPET
GTIRLSAEQA GGNILIIVED DGQGINRERV LEIARERGVV APDQQLTDEQ IDNLIFAPGF
STASEVSDIS GRGVGMDVVL SNIKKIGGSV HVRSWTGKGT RMTLRLPLTL AVLDVMLVKV
ATSPYVIPLS SIVETIQNSR ADFGYMPSGG RVLQVRGEYV QVVDLAQRFE MSSDQSEDNR
FVVLCEAEGN SKIALIVDDI IGQQQVVIKS LEENFERIDG IAGGTILGDG NVALIVDVQS
LKVDSAHQNA A
//
