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Database: UniProt
Entry: A8FX17_SHESH
LinkDB: A8FX17_SHESH
Original site: A8FX17_SHESH 
ID   A8FX17_SHESH            Unreviewed;       690 AA.
AC   A8FX17;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   24-JAN-2024, entry version 82.
DE   SubName: Full=Conserved hypothetical methyl-accepting chemotaxisprotein {ECO:0000313|EMBL:ABV37390.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Ssed_2783 {ECO:0000313|EMBL:ABV37390.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV37390.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV37390.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV37390.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) 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; CP000821; ABV37390.1; -; Genomic_DNA.
DR   RefSeq; WP_012143120.1; NC_009831.1.
DR   AlphaFoldDB; A8FX17; -.
DR   STRING; 425104.Ssed_2783; -.
DR   KEGG; sse:Ssed_2783; -.
DR   eggNOG; COG0840; Bacteria.
DR   eggNOG; COG4564; Bacteria.
DR   HOGENOM; CLU_000445_107_19_6; -.
DR   OMA; GFTSYYF; -.
DR   OrthoDB; 2489132at2; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProt.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd11386; MCP_signal; 1.
DR   CDD; cd12912; PDC2_MCP_like; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR004010; Double_Cache_2.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   InterPro; IPR033480; sCache_2.
DR   PANTHER; PTHR32089:SF55; METHYL ACCEPTING SENSORY TRANSDUCER WITH CACHE_2 SMALL MOLECULE BINDING DOMAIN; 1.
DR   PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR   Pfam; PF08269; dCache_2; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   SMART; SM01049; Cache_2; 2.
DR   SMART; SM00304; HAMP; 1.
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   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002015};
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        339..361
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          358..412
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          417..653
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
SQ   SEQUENCE   690 AA;  75324 MW;  2D3B009E34500148 CRC64;
     MKMTIKVKLI ATVCVALLAI SAFFITNMIS TEVAVLEEQE KNVTDKVELL INDKLKGQVD
     SITLSISGLY EQSKVTNIKS ALQAELTTFT DTIKSIYNTS ASHEEAEIAV YAFINGYRWD
     NGRYIFAYDA DSIVNVANGA HKSYIGKNEK DATDKKGNYY GRDIVNAAKR QEVGFTSYYF
     LNETSGKVEE KISASFYFRP MNLVIATGEY VSTLKQDMID EVLKNITASK YGKNGYFWIQ
     DNQGKILAHP KQEVVGKTLK STKQSVASLR GKDDAFVRME FENPQTGQTE QKIGYVRRIL
     PEWGWIIGTG AYLNDVTVIQ ESLTNATEEI FTEKVTQSII FAAVLFIFAL LASVWVVSHI
     IKELVILKDR IDTLSTGEAD LTSRLDIHSN DEVGDISQSV NNFIGYLQSM MLEISQATVQ
     ITEDILQLNA QSERNNVALN THSSETELAV TAITEMSSTA DTVAQSAVQT ASNTQSANEE
     AMAAKEIVSD ASSSVMALVN EVDEASTRIH TMNTNTQQIV SVLGVIGGIA DQTNLLALNA
     AIEAARAGEQ GRGFAVVADE VRTLAARTQD STAEIDVILS RLTQDAAGAV EVMDATKKSC
     QQAAEKTSRV TESLDIMSDS VVLINDLSSQ IATASEEQSS VTEEINRNMC TIQATVQELT
     QNGVEAAEST HNLAAANEQL TALVSKFKLS
//
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