ID T0PET7_9CLOT Unreviewed; 820 AA.
AC T0PET7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=M918_03825 {ECO:0000313|EMBL:EQB88533.1};
OS Clostridium sp. BL8.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1354301 {ECO:0000313|EMBL:EQB88533.1, ECO:0000313|Proteomes:UP000015873};
RN [1] {ECO:0000313|EMBL:EQB88533.1, ECO:0000313|Proteomes:UP000015873}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BL8 {ECO:0000313|EMBL:EQB88533.1,
RC ECO:0000313|Proteomes:UP000015873};
RX PubMed=25076986; DOI=10.1186/1757-4749-6-30;
RA Marathe N.P., Shetty S.A., Lanjekar V.B., Rasane M.H., Ranade D.R.,
RA Shouche Y.S.;
RT "Genome sequencing of multidrug resistant novel Clostridium sp. BL8 reveals
RT its potential for pathogenicity.";
RL Gut Pathog. 6:30-30(2014).
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:EQB88533.1}.
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DR EMBL; AUPA01000098; EQB88533.1; -; Genomic_DNA.
DR RefSeq; WP_021282960.1; NZ_AUPA01000098.1.
DR AlphaFoldDB; T0PET7; -.
DR STRING; 1354301.M918_03825; -.
DR PATRIC; fig|1354301.3.peg.1851; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000015873; 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; 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; 2.
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; 2.
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; 2.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000015873};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..103
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 445..691
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 693..820
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 419..444
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 820 AA; 91535 MW; DF6FA9C36626E0FA CRC64;
MDTSQYLSMF LEESSDNLQT LNECLLALEN EPRDMEKLNE IFRVAHTIKG MAATMGYSKM
AELTHKMEDV LSNFREGKVK VTHKVVTVLF KCLDTLESMV DSISDGEDGD MPIEDIVSHL
EGIANGTEDG METTIVKENI VEDITNKDTS SQYGIDLNEY ELNIVKQAKY SNVNAYHINI
TLDEGTILKS ARAFVLFQTL EKNGEIIKSV PVLEDLEAEN FDFNIDLVYL SSQTIKEIEK
EIKSITEISR FQLVSLNDGL KVEESNNEQT NMNLNEYELN ILKQAKHSNV NGYHIHITLD
EGTILKSARS FIVFQTLEQS GEIIKSIPAL EDLETENFDL DIDLVYLSSK TATEIEKEIN
NISEIRKVQV FSIDSNSKST ENNESVISAS GSLASMEKAN LKEIEKEKSL ESKIKEKKPI
TEEIKSKPVE QPSQNGQDKK VKAKGIGQSV RVDLDRLDKF MNMVSELVIH RTRLEQISSN
HKIAELNETL EQVARTTTDL QDLVMKIRML PLDVVFNRFP RMIRDLSLEL GKEIELVIQG
QDTELDRTVI EEIGEPLIHL LRNAADHGIE TTEERKAKGK DHTGKIKLVA YSEGTKAVIK
VEDDGKGLDV NKIMAKAEKI GINTEGMSQA DIKNLIFAQG FSTNEVVTDI SGRGVGMDVV
KTKISSLGGT VDAISEEGKG TSFIIRLPLT LQIIQALLVK VGAETMAISL GFIDRVIEYK
EENIRRTNNK EVVLYNGNVI SIIRVNNKLG LESVDQGKKY IILVKVGERE MGLVVDSLLG
QQEIVIKPFG KTLRSTKEYI GATILGDGLV TLILDVAALI
//
