ID A0A1N6N732_9SPIO Unreviewed; 715 AA.
AC A0A1N6N732;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05920897_10184 {ECO:0000313|EMBL:SIP87855.1};
OS Alkalispirochaeta americana.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC Alkalispirochaeta.
OX NCBI_TaxID=159291 {ECO:0000313|EMBL:SIP87855.1, ECO:0000313|Proteomes:UP000186400};
RN [1] {ECO:0000313|EMBL:SIP87855.1, ECO:0000313|Proteomes:UP000186400}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ASpG1 {ECO:0000313|EMBL:SIP87855.1,
RC ECO:0000313|Proteomes:UP000186400};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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};
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DR EMBL; FTMS01000001; SIP87855.1; -; Genomic_DNA.
DR RefSeq; WP_076487320.1; NZ_FTMS01000001.1.
DR AlphaFoldDB; A0A1N6N732; -.
DR STRING; 159291.SAMN05920897_10184; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000186400; 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; 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 InterPro; IPR037257; T2SS_E_N_sf.
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; SSF160246; EspE N-terminal domain-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 Kinase {ECO:0000313|EMBL:SIP87855.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000186400};
KW Transferase {ECO:0000313|EMBL:SIP87855.1}.
FT DOMAIN 1..101
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 338..579
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 581..713
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 121..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 44
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 715 AA; 79255 MW; 2DBEC579B6B57105 CRC64;
MDFSSEPFCI ETRELLKKLE QDLVTLEENP RDEELLNRIF RNVHTMKGSG SMFGFENISE
QAHVMESVFD SLRSGALQVT KEIIDASFEG LDRIEVMLDD PDCRADTGRW RDILDLLPSR
TEEQPPLAEA AGGSASPDSS RGGALQDGSG RPGLEKQDQR KRKKGPLTVF HIRLRPKESA
LQSGNSVIPL FRELAELGEL LIFANDRRLP AWKELKPTHC YIDFDILLSS TAVKETVEEV
FIFIAAHSAV EVTPVAFVEE GDDPPRLGEI LQRRCNLSEE HVEKLLEEQK KNKRLGELAI
EKGYARESDV AVSLEAQNFF KDQHKKHQQK VQSSSLMVPD HKINSAVNLV GELVTLKERL
LRRASELKDP ALNTIAENLN FLTGDLREGI MEMRLVPLQD TFVSFRRLVR DISQDMGKKV
DLQVEGGDTE LDKNVIDVLK SSLVHMIRNS VDHGIESPEE RVAAGKSPVG EILLRAQYVG
SQVQIEVCDD GRGINLEKVR KKAVERGVLP PEAELKMEEV LSILAAPGFS TADQVSSVSG
RGVGTDAVLT EVERLSGQLF LESEQGRGST FTIRLPLTLA IIDSLLVRLD RKFFTIHLND
VKECFILRDA PALLGQGQQV INHEGHPLPL VNLRRHMKMG GDVPDIANVV VVDSGSQRAG
IVVDQIMGQS QVVIKPLNGA VRTVPEISGS TILGDGSISF ILDVPRMITG LYAPR
//
