ID A0A1M6EHW0_PSEXY Unreviewed; 707 AA.
AC A0A1M6EHW0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN02745725_01221 {ECO:0000313|EMBL:SHI85066.1};
OS Pseudobutyrivibrio xylanivorans DSM 14809.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Pseudobutyrivibrio.
OX NCBI_TaxID=1123012 {ECO:0000313|EMBL:SHI85066.1, ECO:0000313|Proteomes:UP000184185};
RN [1] {ECO:0000313|EMBL:SHI85066.1, ECO:0000313|Proteomes:UP000184185}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14809 {ECO:0000313|EMBL:SHI85066.1,
RC ECO:0000313|Proteomes:UP000184185};
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; FQYQ01000006; SHI85066.1; -; Genomic_DNA.
DR RefSeq; WP_072914349.1; NZ_FQYQ01000006.1.
DR AlphaFoldDB; A0A1M6EHW0; -.
DR STRING; 185007.SAMN02910350_01268; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000184185; 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; 2.40.50.180; CheA-289, Domain 4; 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 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:SHI85066.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000184185};
KW Transferase {ECO:0000313|EMBL:SHI85066.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..103
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 368..577
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 579..707
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 130..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 46
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 707 AA; 76378 MW; 095C664730194843 CRC64;
MDVSQYLDIF IDETSGHIQS LSDNIMELEK EPDNKDVVNE IFRAAHSLKG MAGTMGFKRM
QRLTHDMENV FQEVRNDNVK VNSALIDILF KCLDAIESYL DTVKATSNEG EEENEALIKL
LNDYLSGGGG EGGGEAAPAA EAPAEAPAEG GGAADGAGGP LYKKIPVDPE LCEKLKGEKQ
LYGFTVHISK ECLLKAARAF LVFKAVEDFG QIMAFNPSSG DIEDENFEFD FSFILSSESE
LDPIIESIKT VSEIESVEAD KVTPEMYEKK EEEAPAAPAE AAAPAPEAAA APAAPAAPAP
AAPAAPAAKS GGGGKTTQPA NKPVTSRTIR VDIEKLDALM NQVSELIIAK NSLASQSNGS
GEIDSQTLHE NIEYLERITT NLHESVMKVR MVPIESVVAK FPRMIRDLDR KLNKPMELVM
TGEDTELDRT VVDQLGDPLQ HLLRNSADHG IESPEDRRAA GKPEKGTIFL NAFQEGNNVI
IEVGDDGGGI NTDKVRDKAV ERGLVTPEEA ENLTQKEIID FLFMPSFSMA KQITDISGRG
VGLDVVKSNI EALGGDVTVK SVMGEGSTFT VRLPLTLAII QALMVEIRDE KYAIALASIM
NIENIPKSEI KYVESKEVIH LRGQVIPLIH LDKLLDFEPK EDTEDTMTVV ICKKGDTLGG
IIVDNLIGQL EIVIKSLGKL DNNKLISGAT ILGDGEIAMI LDVNAVI
//
