ID A0A101FP82_9FIRM Unreviewed; 322 AA.
AC A0A101FP82;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=CheW domain protein {ECO:0000313|EMBL:KUK40652.1};
DE Flags: Fragment;
GN ORFNames=XD69_1301 {ECO:0000313|EMBL:KUK40652.1};
OS Clostridia bacterium 62_21.
OC Bacteria; Bacillota; Clostridia.
OX NCBI_TaxID=1635276 {ECO:0000313|EMBL:KUK40652.1, ECO:0000313|Proteomes:UP000067139};
RN [1] {ECO:0000313|EMBL:KUK40652.1, ECO:0000313|Proteomes:UP000067139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=62_21 {ECO:0000313|EMBL:KUK40652.1};
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
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:KUK40652.1}.
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DR EMBL; LGFR01000159; KUK40652.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101FP82; -.
DR PATRIC; fig|1635276.4.peg.554; -.
DR Proteomes; UP000067139; 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; 3.30.70.1110; Histidine kinase CheA-like, P2 response regulator-binding 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; IPR035891; CheY-binding_CheA.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR036641; HPT_dom_sf.
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; PF02895; H-kinase_dim; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF07194; P2; 1.
DR SMART; SM01231; H-kinase_dim; 1.
DR SMART; SM00073; HPT; 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; PS50894; HPT; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110}.
FT DOMAIN 1..103
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 46
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT NON_TER 322
FT /evidence="ECO:0000313|EMBL:KUK40652.1"
SQ SEQUENCE 322 AA; 34865 MW; C72A7974EAD41D67 CRC64;
MFSDAELQVF LDELDEKIQI INDNLLVLER DPSDTGALQE IFRAAHTIKG SAGVMGYEHM
ASLTHEMENL FDCLRQGTMR LTPEMTDVLF NALDTLKALR DEVTGGAGAT DTAPVIGKLR
AFLAGEQEGA PAAAAAGKAA ESAAAPPASF AALTEAEQEV IRAAAARNIN AYHIRVLIDP
QCQMKSVRAF LVFNNLERFG EIIKSVPAAE ELQEGRYGEG FEVVLLAGDE PDYIRNMLMT
IAEVTDAEVV PLRPEEAAAA PPAGETAQAK EAPAAQATVQ KVHTVRTVRV DVEKMDNLMN
LVGELVIERT RLDRFAALLR AH
//