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Database: UniProt
Entry: A0A1M4TEZ1_9FIRM
LinkDB: A0A1M4TEZ1_9FIRM
Original site: A0A1M4TEZ1_9FIRM 
ID   A0A1M4TEZ1_9FIRM        Unreviewed;       689 AA.
AC   A0A1M4TEZ1;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN02745190_00459 {ECO:0000313|EMBL:SHE43023.1};
OS   Schwartzia succinivorans DSM 10502.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC   Schwartzia.
OX   NCBI_TaxID=1123243 {ECO:0000313|EMBL:SHE43023.1, ECO:0000313|Proteomes:UP000184404};
RN   [1] {ECO:0000313|EMBL:SHE43023.1, ECO:0000313|Proteomes:UP000184404}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10502 {ECO:0000313|EMBL:SHE43023.1,
RC   ECO:0000313|Proteomes:UP000184404};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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; FQUG01000002; SHE43023.1; -; Genomic_DNA.
DR   RefSeq; WP_072934549.1; NZ_FQUG01000002.1.
DR   AlphaFoldDB; A0A1M4TEZ1; -.
DR   STRING; 1123243.SAMN02745190_00459; -.
DR   OrthoDB; 9803176at2; -.
DR   Proteomes; UP000184404; 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   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; 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; 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:SF1; 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; 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; 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   Kinase {ECO:0000313|EMBL:SHE43023.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184404};
KW   Transferase {ECO:0000313|EMBL:SHE43023.1};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          1..103
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   DOMAIN          344..557
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          559..689
FT                   /note="CheW-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50851"
FT   REGION          273..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         46
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   689 AA;  74208 MW;  7EBA87979432DF88 CRC64;
     MDTNQYMEMF LEESREHLQS LNDGLLGLEN DPEDLSILND IFRNAHTIKG MSATMGYTKI
     AELTHDTENV LDLLRKEQLK VSEDIVDTLF KCVDSLEQMV ESIGEGGPED VVDVTEIAAK
     LSALVKGEAA PAAAAAAPAA PAAEAPAAPS IEYDDTDKDV INQALGSGMR VLHINVALTE
     SCVLKSARSY MVMNALDQLG DVMKSIPPAE DLEQEKFEHS FDVVFVTDAE PSTVEETLMA
     ISEVDKVVIT DVAEELKAQE AAAKAPAAPA PAAAPAAAPA PAPAAAKPAP AKKAAAPAKG
     AEKKAPKGSQ SVRVDIEKLD NLLNLVGELV INKVRLEQIG ITHRLAELTE TLEQMDRVTT
     DLQTVVMKVR MVPVGQVFNR FPRMVRDLAK ELNKEINLTI EGEETELDRT VIDEIGDPLM
     HLLRNSLDHG VEHPDDREAK GKPRSGEVAL IARHEGNNVV IMVTDDGKGI NADAIRRKAV
     EKGMISQEEA DSLNDADAVR LIFLPGFSTA ETITDVSGRG VGMDVVRSKI ETLGGHVDVE
     TKVDEGSVFK IKLPLTLAII QALLVKVQEE MYAIPLGSID STINIKQEDI KTVQNKEVIV
     LRGQIIPIIR LGNILNVPTQ EGEENDDIFV VVVHLGERKA GIVVDNLIGQ QEIVIKTLGK
     LLAGLKVISG ATVLGDGRVA LILDVSALM
//
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