ID A0A1Y0G914_9PROT Unreviewed; 545 AA.
AC A0A1Y0G914;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Methyl-accepting chemotaxis protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CAP31_11115 {ECO:0000313|EMBL:ARU32180.1};
OS Sulfuriferula sp. AH1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Sulfuricellaceae; Sulfuriferula.
OX NCBI_TaxID=1985873 {ECO:0000313|EMBL:ARU32180.1, ECO:0000313|Proteomes:UP000195558};
RN [1] {ECO:0000313|EMBL:ARU32180.1, ECO:0000313|Proteomes:UP000195558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AH1 {ECO:0000313|EMBL:ARU32180.1,
RC ECO:0000313|Proteomes:UP000195558};
RA Jones D.S., Hua A.A., Roepke E.W., Bailey J.V.;
RT "The complete genome sequence of Sulfuriferula sp. str. AH1, a sulfur-
RT oxidizing autotroph isolated from weathered sulfide-bearing rock from the
RT Duluth Complex.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
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DR EMBL; CP021138; ARU32180.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0G914; -.
DR KEGG; sulf:CAP31_11115; -.
DR OrthoDB; 8899037at2; -.
DR Proteomes; UP000195558; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd06225; HAMP; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR024478; HlyB_4HB_MCP.
DR InterPro; IPR004089; MCPsignal_dom.
DR PANTHER; PTHR32089:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 1.
DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR Pfam; PF12729; 4HB_MCP_1; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00304; HAMP; 2.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000195558};
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 13..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 195..218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 215..268
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 273..509
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 545 AA; 58632 MW; 712F76709FE68986 CRC64;
MKWFLNLSMR NKLFLGFGIM IVFVGIVIAT GYFAIARLQV AQQALYQKDF ANLRDLTNLR
SFQSQMRAEI LEAQLINTAD ERERLMKDMA EYAGQVDKIM AVLLSRASND PKLLSRLEEL
NIIQKAFAQT RDSEIVPLIR AGKITESRQL VVGIQRDRYE KIRSIINELN HEADKNAHRA
VAESGLAADS ALHQFIMVGV GAILLAVIMT LLTGRIIAAP LQMVSSIAGR VAAGDLTVDI
PDGNRTDEVG ELLRAFSAML EGLRTLMREI NDGVGVLASS SGEILATTTQ VASGAAETAS
AVNETTVTVE EVKQTAQLAS QKARFVSDSA QKASQVSQNG RKAVEDAMQG MQNIQEQMES
IAESIVRLSE QSQAIGEIIA TVNDLAEQSN LLAVNAAIEA NKAGEQGKGF AVVAQEVKSL
AEQSKQATAQ VRTILGDIQR ATTATVLATE QGNKAVQAGV KQTGETGEAI RQLADSANEA
AQAATQIAAS SQQQMVGMDQ VALAMENIKQ ASAQNVSGTR QAEVAARSLH ELGQKLQQLA
TQYRV
//
