ID Q8RBX6_CALS4 Unreviewed; 602 AA.
AC Q8RBX6;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 122.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:AAM23944.1};
GN Name=Tar4 {ECO:0000313|EMBL:AAM23944.1};
GN OrderedLocusNames=TTE0680 {ECO:0000313|EMBL:AAM23944.1};
OS Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM
OS 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Caldanaerobacter.
OX NCBI_TaxID=273068 {ECO:0000313|EMBL:AAM23944.1, ECO:0000313|Proteomes:UP000000555};
RN [1] {ECO:0000313|EMBL:AAM23944.1, ECO:0000313|Proteomes:UP000000555}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4
RC {ECO:0000313|Proteomes:UP000000555};
RX PubMed=11997336; DOI=10.1101/gr.219302;
RA Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y.,
RA Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R.,
RA Wang J., Yu J., Yang H.;
RT "A complete sequence of the T. tengcongensis genome.";
RL Genome Res. 12:689-700(2002).
RN [2] {ECO:0007829|PDB:1U4H, ECO:0007829|PDB:1U55}
RP X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 1-188 IN COMPLEX WITH HEME B.
RX PubMed=15326296; DOI=10.1073/pnas.0405188101;
RA Pellicena P., Karow D.S., Boon E.M., Marletta M.A., Kuriyan J.;
RT "Crystal structure of an oxygen-binding heme domain related to soluble
RT guanylate cyclases.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:12854-12859(2004).
RN [3] {ECO:0007829|PDB:1XBN}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-191 IN COMPLEX WITH HEME B.
RX PubMed=15472039; DOI=10.1126/science.1103596;
RA Nioche P., Berka V., Vipond J., Minton N., Tsai A.L., Raman C.S.;
RT "Femtomolar sensitivity of a NO sensor from Clostridium botulinum.";
RL Science 306:1550-1553(2004).
RN [4] {ECO:0007829|PDB:3EEE}
RP X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 1-188 IN COMPLEX WITH HEME B.
RX PubMed=19032091; DOI=10.1021/cb800185h;
RA Olea C., Boon E.M., Pellicena P., Kuriyan J., Marletta M.A.;
RT "Probing the function of heme distortion in the H-NOX family.";
RL ACS Chem. Biol. 3:703-710(2008).
RN [5] {ECO:0007829|PDB:3IQB}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-188 IN COMPLEX WITH HEME B.
RX PubMed=20017169; DOI=10.1002/anie.200904799;
RA Weinert E.E., Plate L., Whited C.A., Olea C., Marletta M.A.;
RT "Determinants of ligand affinity and heme reactivity in H-NOX domains.";
RL Angew. Chem. Int. Ed. 49:720-723(2010).
RN [6] {ECO:0007829|PDB:3M0B}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-188.
RX PubMed=20373741; DOI=10.1021/ja101527r;
RA Winter M.B., McLaurin E.J., Reece S.Y., Olea C., Nocera D.G.,
RA Marletta M.A.;
RT "Ru-porphyrin protein scaffolds for sensing O2.";
RL J. Am. Chem. Soc. 132:5582-5583(2010).
RN [7] {ECO:0007829|PDB:3NVR, ECO:0007829|PDB:3NVU}
RP X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) OF 1-188 IN COMPLEX WITH HEME B.
RX PubMed=20735135; DOI=10.1021/ja106252b;
RA Olea C., Kuriyan J., Marletta M.A.;
RT "Modulating heme redox potential through protein-induced porphyrin
RT distortion.";
RL J. Am. Chem. Soc. 132:12794-12795(2010).
RN [8] {ECO:0007829|PDB:3LAH, ECO:0007829|PDB:3LAI}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-188 IN COMPLEX WITH HEME B.
RX PubMed=20162612; DOI=10.1002/pro.357;
RA Olea C., Herzik M.A., Kuriyan J., Marletta M.A.;
RT "Structural insights into the molecular mechanism of H-NOX activation.";
RL Protein Sci. 19:881-887(2010).
RN [9] {ECO:0007829|PDB:3SJ5}
RP X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 1-188 IN COMPLEX WITH HEME B.
RX PubMed=21721586; DOI=10.1021/bi200788x;
RA Weinert E.E., Phillips-Piro C.M., Tran R., Mathies R.A., Marletta M.A.;
RT "Controlling conformational flexibility of an O-binding H-NOX domain.";
RL Biochemistry 50:6832-6840(2011).
RN [10] {ECO:0007829|PDB:3TF0, ECO:0007829|PDB:3TF1}
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 1-188 IN COMPLEX WITH HEME B.
RX PubMed=21997213; DOI=10.1073/pnas.1114038108;
RA Winter M.B., Herzik M.A., Kuriyan J., Marletta M.A.;
RT "Tunnels modulate ligand flux in a heme nitric oxide/oxygen binding (H-NOX)
RT domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:E881-E889(2011).
RN [11] {ECO:0007829|PDB:4IT2}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-188.
RX PubMed=23394479; DOI=10.1021/ic302685h;
RA Winter M.B., Klemm P.J., Phillips-Piro C.M., Raymond K.N., Marletta M.A.;
RT "Porphyrin-substituted H-NOX proteins as high-relaxivity MRI contrast
RT agents.";
RL Inorg. Chem. 52:2277-2279(2013).
RN [12] {ECO:0007829|PDB:4FDK}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-188 IN COMPLEX WITH HEME B.
RX PubMed=23831583; DOI=10.1016/j.jinorgbio.2013.06.004;
RA Weinert E.E., Phillips-Piro C.M., Marletta M.A.;
RT "Porphyrin pi-stacking in a heme protein scaffold tunes gas ligand
RT affinity.";
RL J. Inorg. Biochem. 127:7-12(2013).
RN [13] {ECO:0007829|PDB:5JRU, ECO:0007829|PDB:5JRV}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-188 IN COMPLEX WITH HEME B.
RX PubMed=27328180; DOI=10.1021/acschembio.6b00431;
RA Hespen C.W., Bruegger J.J., Phillips-Piro C.M., Marletta M.A.;
RT "Structural and Functional Evidence Indicates Selective Oxygen Signaling in
RT Caldanaerobacter subterraneus H-NOX.";
RL ACS Chem. Biol. 11:2337-2346(2016).
RN [14] {ECO:0007829|PDB:6CWW}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-188 IN COMPLEX WITH HEME B.
RX PubMed=29780583; DOI=10.1039/c8ra02000k;
RA Kearney C., Olenginski L.T., Hirn T.D., Fowler G.D., Tariq D., Brewer S.H.,
RA Phillips-Piro C.M.;
RT "Exploring local solvation environments of a heme protein using the
RT spectroscopic reporter 4-cyano-l-phenylalanine.";
RL RSC Adv. 8:13503-13512(2018).
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DR EMBL; AE008691; AAM23944.1; -; Genomic_DNA.
DR RefSeq; WP_011025086.1; NZ_JANUCV010000001.1.
DR PDB; 1U4H; X-ray; 2.07 A; A/B=1-188.
DR PDB; 1U55; X-ray; 1.77 A; A/B=1-188.
DR PDB; 1U56; X-ray; 1.90 A; A/B=1-188.
DR PDB; 1XBN; X-ray; 2.50 A; A=1-191.
DR PDB; 3EEE; X-ray; 2.12 A; A/B/C/D=1-188.
DR PDB; 3IQB; X-ray; 2.10 A; A=1-188.
DR PDB; 3LAH; X-ray; 2.00 A; A/B=1-188.
DR PDB; 3LAI; X-ray; 2.14 A; A/B/C=1-188.
DR PDB; 3M0B; X-ray; 2.00 A; A=1-188.
DR PDB; 3NVR; X-ray; 2.15 A; A/B=1-188.
DR PDB; 3NVU; X-ray; 2.04 A; A/B=1-188.
DR PDB; 3SJ5; X-ray; 1.67 A; A/B=1-188.
DR PDB; 3TF0; X-ray; 1.74 A; A/B=1-188.
DR PDB; 3TF1; X-ray; 2.04 A; A/B=1-188.
DR PDB; 4FDK; X-ray; 2.10 A; A/B=1-188.
DR PDB; 4IT2; X-ray; 2.10 A; A/B=1-188.
DR PDB; 5JRU; X-ray; 2.31 A; A/B/C/D/E/F=1-188.
DR PDB; 5JRV; X-ray; 1.95 A; A/B=1-188.
DR PDB; 5JRX; X-ray; 1.95 A; A/B=1-188.
DR PDB; 6CWW; X-ray; 1.85 A; A/B=1-188.
DR PDBsum; 1U4H; -.
DR PDBsum; 1U55; -.
DR PDBsum; 1U56; -.
DR PDBsum; 1XBN; -.
DR PDBsum; 3EEE; -.
DR PDBsum; 3IQB; -.
DR PDBsum; 3LAH; -.
DR PDBsum; 3LAI; -.
DR PDBsum; 3M0B; -.
DR PDBsum; 3NVR; -.
DR PDBsum; 3NVU; -.
DR PDBsum; 3SJ5; -.
DR PDBsum; 3TF0; -.
DR PDBsum; 3TF1; -.
DR PDBsum; 4FDK; -.
DR PDBsum; 4IT2; -.
DR PDBsum; 5JRU; -.
DR PDBsum; 5JRV; -.
DR PDBsum; 5JRX; -.
DR PDBsum; 6CWW; -.
DR AlphaFoldDB; Q8RBX6; -.
DR SMR; Q8RBX6; -.
DR STRING; 273068.TTE0680; -.
DR KEGG; tte:TTE0680; -.
DR eggNOG; COG0840; Bacteria.
DR HOGENOM; CLU_000445_107_18_9; -.
DR OrthoDB; 3192at2; -.
DR EvolutionaryTrace; Q8RBX6; -.
DR Proteomes; UP000000555; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1520.10; H-NOX domain; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR038158; H-NOX_domain_sf.
DR InterPro; IPR011644; Heme_NO-bd.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR024096; NO_sig/Golgi_transp_ligand-bd.
DR PANTHER; PTHR32089:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 1.
DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR Pfam; PF07700; HNOB; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF111126; Ligand-binding domain in the NO signalling and Golgi transport; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:1U4H, ECO:0007829|PDB:1U55};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Heme {ECO:0007829|PDB:1U4H, ECO:0007829|PDB:1U55};
KW Iron {ECO:0007829|PDB:1U4H, ECO:0007829|PDB:1U55};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0007829|PDB:1U4H, ECO:0007829|PDB:1U55};
KW Reference proteome {ECO:0000313|Proteomes:UP000000555};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW ProRule:PRU00284}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 206..224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 230..247
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 316..573
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT COILED 569..596
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 2
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:1U4H, ECO:0007829|PDB:1U56"
FT BINDING 2
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:3LAH, ECO:0007829|PDB:3LAI"
FT BINDING 78
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:1U55, ECO:0007829|PDB:1U56"
FT BINDING 102
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /ligand_part_note="axial binding residue"
FT /evidence="ECO:0007829|PDB:1U4H, ECO:0007829|PDB:1U55"
FT BINDING 113
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:3LAH, ECO:0007829|PDB:3LAI"
FT BINDING 113
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:1U55, ECO:0007829|PDB:1U56"
FT BINDING 131
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:1U4H, ECO:0007829|PDB:1U55"
FT BINDING 131
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:3LAH, ECO:0007829|PDB:3LAI"
FT BINDING 133
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /ligand_note="covalent"
FT /evidence="ECO:0007829|PDB:5JRV"
FT BINDING 133
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:3LAH, ECO:0007829|PDB:3LAI"
FT BINDING 135
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:1U4H, ECO:0007829|PDB:1U55"
FT BINDING 135
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:3LAI"
SQ SEQUENCE 602 AA; 68053 MW; 6CD008747FCBC22E CRC64;
MKGTIVGTWI KTLRDLYGND VVDESLKSVG WEPDRVITPL EDIDDDEVRR IFAKVSEKTG
KNVNEIWREV GRQNIKTFSE WFPSYFAGRR LVNFLMMMDE VHLQLTKMIK GATPPRLIAK
PVAKDAIEME YVSKRKMYDY FLGLIEGSSK FFKEEISVEE VERGEKDGFS RLKVRIKFKN
PVFEYKKNVW GKILGFGFIR SNSFKLALWS FIIGFLVVGF VSSWDLLKSF SGAFIIGAFT
YIFSYILNMP AKNLHEFVKI MGSRNLEEEF KLESGDVFEA IAEELNSVKD TIKKDMLFLK
GGTDDMHNFV HRFNEIAENM KKVSEDISSV VNDVASSTVH QAEEIERAVG ILDENIKKIN
EIAGTSKESN EKLENSIENI KRANTDVTDV AKELSQVEVD FSSIYEMGKV LSDSAKDIMA
IVTTVEEISD QTNLLALNAA IEAARAGEAG RGFAVVAEEV RNLAENSKNA VKTITESLVN
FTGQVENLAE KISAQFERLK KSISTLEKVV EKNTMATEEV AGISSVIVES ANRLYEEAEK
LSEVFGHLEN LAAISEENSA SSEEMSANVT EYSNRIREFI EQIKQMETLV TNFKKELDKY
KV
//
