ID   Q21YP5_ALBFT            Unreviewed;       759 AA.
AC   Q21YP5;
DT   18-APR-2006, integrated into UniProtKB/TrEMBL.
DT   18-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   SubName: Full=Methyl-accepting chemotaxis sensory transducer {ECO:0000313|EMBL:ABD69108.1};
GN   OrderedLocusNames=Rfer_1374 {ECO:0000313|EMBL:ABD69108.1};
OS   Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118)
OS   (Rhodoferax ferrireducens).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=338969 {ECO:0000313|EMBL:ABD69108.1, ECO:0000313|Proteomes:UP000008332};
RN   [1] {ECO:0000313|Proteomes:UP000008332}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-621 / DSM 15236 / T118
RC   {ECO:0000313|Proteomes:UP000008332};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236.";
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000256|ARBA:ARBA00029447}.
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DR   EMBL; CP000267; ABD69108.1; -; Genomic_DNA.
DR   RefSeq; WP_011463676.1; NC_007908.1.
DR   AlphaFoldDB; Q21YP5; -.
DR   STRING; 338969.Rfer_1374; -.
DR   KEGG; rfr:Rfer_1374; -.
DR   eggNOG; COG0840; Bacteria.
DR   HOGENOM; CLU_000445_107_27_4; -.
DR   Proteomes; UP000008332; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; cd11386; MCP_signal; 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; IPR004089; MCPsignal_dom.
DR   InterPro; IPR029095; NarX-like_N.
DR   PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR   PANTHER; PTHR32089:SF119; METHYL-ACCEPTING CHEMOTAXIS PROTEIN TLPQ; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   Pfam; PF13675; PilJ; 2.
DR   PRINTS; PR00260; CHEMTRNSDUCR.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008332};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW   ProRule:PRU00284};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        90..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          433..481
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          486..722
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
FT   REGION          42..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          399..438
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        42..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   759 AA;  80588 MW;  55711F85FE23DC95 CRC64;
     MSVVDQLKNF FVKKVPESDQ DSRLSLGVPG ATLYPMELDQ MTGTTESGQQ RPVAPGRSSG
     DTGEAIDDEA ANLIALPILG KKTVVQHQRL LSILLGLALV LLVVVTLFAL NQANKVAQQL
     GATGQSLMQS QRLAKSVSQA LVGGAEAFPD VVESSGVLAK SVRGLKAGDG QMGLSALSPD
     YLPELDKITP LMERAEKNAA IVLGQQKILT QVGAALRLIN RQSSDLLEIA ETASSLKLQQ
     NAAAAEISAA GQLVMLTQRI GKSSNEFLTV EGVSPEAVFL LGKDLNSFKE IAQGMLDGSP
     ELRLGATKDP QTREQLAALI NLFEETRKQA GAILGNLQGL VSAREAQVSI IADSEPLRRN
     LEELQGKLSA HAGLGAGALS MLVGSVLLAL LCAGGLSYVQ LLDSRKRQVA AEAQRLEAER
     QEKEAKRVND ANQAAILRLM NELQTVAEGD LTQEATVTED ITGAIADSVN YTVEELRSLV
     GNVQSTVTRV AQTTAEVDTT STELLAASNE QLHEIRETGR SVVDMASRIN DVSVQAQESA
     SVARQSLQAA EVGLKAVQNT IGGMNSIRDQ IQETSKRIKR LGESSQEIGE ITELISDITE
     QTNVLALNAA IQAASAGEAG RGFSVVAEEV QRLAERSADA TRQISALVKA IQTDTQDAVG
     AMERSTQGVV EGAKLSDNAG TALTEIDQVS RRLAELIEQI SSSTSREANL ANVVADNIQH
     IFAVTEQTGE GTRSTAAQVR ELSKMAEELR QSVSRFKIA
//