ID W0DZ03_9GAMM Unreviewed; 722 AA.
AC W0DZ03;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Methyl-accepting chemotaxis protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=THIAE_02750 {ECO:0000313|EMBL:AHF02199.1};
OS Thiomicrospira aerophila AL3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Thiomicrospira.
OX NCBI_TaxID=717772 {ECO:0000313|EMBL:AHF02199.1, ECO:0000313|Proteomes:UP000005380};
RN [1] {ECO:0000313|EMBL:AHF02199.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AL3 {ECO:0000313|EMBL:AHF02199.1};
RG DOE Joint Genome Institute;
RA Kappler U., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (DEC-2013) 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; CP007030; AHF02199.1; -; Genomic_DNA.
DR RefSeq; WP_006459969.1; NZ_CP007030.1.
DR AlphaFoldDB; W0DZ03; -.
DR STRING; 717772.THIAE_02750; -.
DR KEGG; tao:THIAE_02750; -.
DR eggNOG; COG0840; Bacteria.
DR HOGENOM; CLU_000445_107_20_6; -.
DR InParanoid; W0DZ03; -.
DR OrthoDB; 6433966at2; -.
DR Proteomes; UP000005380; Chromosome.
DR GO; GO:0016020; C: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 Gene3D; 1.20.120.1530; -; 2.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR024478; HlyB_4HB_MCP.
DR InterPro; IPR004089; MCPsignal_dom.
DR PANTHER; PTHR43531:SF14; METHYL-ACCEPTING CHEMOTAXIS PROTEIN I-RELATED; 1.
DR PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR Pfam; PF12729; 4HB_MCP_1; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF18947; HAMP_2; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR SMART; SM00304; HAMP; 2.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 2.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 2.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 181..200
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 206..259
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 377..436
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 441..670
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT REGION 693..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 460..490
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 722 AA; 78266 MW; 06A5E512F2010A2B CRC64;
MSIKNSITLL VSTLLGFALL AVVLGLVSMK VNNDNLHELY DDRVVPLQGL KEIADSYAVN
IVDTNHKLRN GNISWQEAEQ NIAQAKRDIR QLWGDYMATT LTPEEAQLAQ RAQSLMEPAD
RAVDELERLV KARDMQGITQ FSIDRLYPVI DPISDAVTDL VNLQLRVAAE LNERNEATYQ
LTFKLAIMAS LIFFALAIFF SRTTLRAVTL PLNELVRVSR HVQEQGDFSA RIKVSRQDEV
GQAANAFNDL LANAAKAITE ANHVVGAIAQ SDFSQRVQGQ YVGDLDKLKQ GVNASAEQVA
FMMDELGKVM QALYNGRFDA KMDERVPQAF SQQVDNALHS IDQVIVDINS VMAYMNEGKF
QHRVKADARG QLSELKGNIN GSMDSLENAV NAITDVVVAQ SNGDLTKRIE GEYHGELRIL
TEAVNNTAVK LTGVVSQAIN ASNIVHTAAD EVSKGALDLS ERVQEQAAAL EETSATMEEM
NSAVQNNTQN AMEATQVVVG VADKASKGKV VMQQTIDAMG AIQESSHKIS DIVNLIDGIA
FQTNLLALNA AVEAARAGDH GRGFAVVAGE VRALAQKSAQ AAKEISTLIS ESVSRVDQGT
KLAFESGDML NQMNDAVQEV TKMIEQIAQA SKEQADGVQQ VHQAISNIDQ VTQQNAALVE
QTSAASESMS EQAAILSNDM VFFNTGNHRQ AAPAKLAAPK SASAPKALPI KPKPAADEWS
EF
//