ID   Q30TY1_SULDN            Unreviewed;       663 AA.
AC   Q30TY1;
DT   06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   06-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   SubName: Full=Methyl-accepting chemotaxis sensory transducer {ECO:0000313|EMBL:ABB43550.1};
GN   OrderedLocusNames=Suden_0269 {ECO:0000313|EMBL:ABB43550.1};
OS   Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) (Thiomicrospira
OS   denitrificans (strain ATCC 33889 / DSM 1251)).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Sulfurimonadaceae; Sulfurimonas.
OX   NCBI_TaxID=326298 {ECO:0000313|EMBL:ABB43550.1, ECO:0000313|Proteomes:UP000002714};
RN   [1] {ECO:0000313|EMBL:ABB43550.1, ECO:0000313|Proteomes:UP000002714}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33889 / DSM 1251 {ECO:0000313|Proteomes:UP000002714};
RX   PubMed=18065616; DOI=10.1128/AEM.01844-07;
RA   Sievert S.M., Scott K.M., Klotz M.G., Chain P.S.G., Hauser L.J., Hemp J.,
RA   Huegler M., Land M., Lapidus A., Larimer F.W., Lucas S., Malfatti S.A.,
RA   Meyer F., Paulsen I.T., Ren Q., Simon J., Bailey K., Diaz E.,
RA   Fitzpatrick K.A., Glover B., Gwatney N., Korajkic A., Long A.,
RA   Mobberley J.M., Pantry S.N., Pazder G., Peterson S., Quintanilla J.D.,
RA   Sprinkle R., Stephens J., Thomas P., Vaughn R., Weber M.J., Wooten L.L.;
RT   "Genome of the epsilonproteobacterial chemolithoautotroph Sulfurimonas
RT   denitrificans.";
RL   Appl. Environ. Microbiol. 74:1145-1156(2008).
CC   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000256|ARBA:ARBA00029447}.
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DR   EMBL; CP000153; ABB43550.1; -; Genomic_DNA.
DR   RefSeq; WP_011371905.1; NC_007575.1.
DR   AlphaFoldDB; Q30TY1; -.
DR   STRING; 326298.Suden_0269; -.
DR   KEGG; tdn:Suden_0269; -.
DR   eggNOG; COG0840; Bacteria.
DR   HOGENOM; CLU_000445_107_19_7; -.
DR   OrthoDB; 9765597at2; -.
DR   Proteomes; UP000002714; 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   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; IPR029150; dCache_3.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   InterPro; IPR029151; Sensor-like_sf.
DR   PANTHER; PTHR32089:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 1.
DR   PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR   Pfam; PF14827; dCache_3; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   PRINTS; PR00260; CHEMTRNSDUCR.
DR   SMART; SM00283; MA; 1.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR   SUPFAM; SSF103190; Sensory domain-like; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002714};
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        7..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        294..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          378..425
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          450..663
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
FT   COILED          574..601
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   663 AA;  74180 MW;  6DF50E495172A128 CRC64;
     MTIGKRVTIL VIGISFALLV SSFFVLNYFK AAIVQNVYSD MRSTLTAKIE DRMNAKFDIG
     VTNAVAMANN SDIIASLKNN DRALAAKTLE SIGDTYKEQT DFKNIKIHIH DKDVKSFLRN
     WQVDKFGDDL SSFRHTINKV KESKKSMAAI EVGRNGLTIR GLVPVIADNS YLGSLEFMQG
     FESVVKQFLK EKEYLLVLMD NKLLNVADLS NTKNRISNYT LSQKTIDDKF LLEAKTIDME
     AVLRDGYFVD KNYFYTYTYI KDFENKPIGI YLLAKDRPSI EKAIDGASSI INSALLLVAS
     LIFIITIAIL VTIKKIVLNP LNVFQEGLLE FFKYLNKQSN KAELIAIDTN DEIGKMAKIV
     NENILKTKEN IELDQDLIND VKRVVMEVER GNLNQEVTKS TQNQALFELK DSLNKMLYSL
     KNSVAKDINS LVAVLDSFKN SDFRATLEND EAKVSQAINS IGQTIRDMLR DSNTNADELT
     RTSVSLIERM QTLAEGSYKQ ASMLKDISKT MELANSSVVE VSQMTKAVVI KSTDIKSVVN
     VISEIADQTN LLALNAAIEA ARAGEHGRGF AVVADEVRKL AENTQRSLDD ININIESLTQ
     AVVDIGTTIE EQVKDINMAT DSIKVIDKTT QEHAIHTKEI ENIAIKLDEM SKKTLQSIST
     KKF
//