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Database: UniProt
Entry: H2CDL6_9LEPT
LinkDB: H2CDL6_9LEPT
Original site: H2CDL6_9LEPT 
ID   H2CDL6_9LEPT            Unreviewed;       532 AA.
AC   H2CDL6;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Methyl-accepting chemotaxis sensory transducer {ECO:0000313|EMBL:EHQ06549.1};
GN   ORFNames=Lepil_1866 {ECO:0000313|EMBL:EHQ06549.1};
OS   Leptonema illini DSM 21528.
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptonema.
OX   NCBI_TaxID=929563 {ECO:0000313|EMBL:EHQ06549.1, ECO:0000313|Proteomes:UP000005737};
RN   [1] {ECO:0000313|EMBL:EHQ06549.1, ECO:0000313|Proteomes:UP000005737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21528 {ECO:0000313|EMBL:EHQ06549.1,
RC   ECO:0000313|Proteomes:UP000005737};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Held B.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E.-M.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The Improved High-Quality Draft genome of Leptonema illini DSM 21528.";
RL   Submitted (OCT-2011) 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; JH597773; EHQ06549.1; -; Genomic_DNA.
DR   RefSeq; WP_002772177.1; NZ_JH597773.1.
DR   AlphaFoldDB; H2CDL6; -.
DR   STRING; 183.GCA_002009735_03200; -.
DR   HOGENOM; CLU_000445_107_27_12; -.
DR   Proteomes; UP000005737; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma 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; cd06225; HAMP; 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   InterPro; IPR000727; T_SNARE_dom.
DR   PANTHER; PTHR32089:SF112; HEME-BASED AEROTACTIC TRANSDUCER HEMAT; 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.
DR   PROSITE; PS50192; T_SNARE; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005737};
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        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        188..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          215..269
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          281..517
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
FT   DOMAIN          433..495
FT                   /note="T-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50192"
FT   COILED          82..116
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   532 AA;  58331 MW;  D6818C6483ACF4CB CRC64;
     MTSFKNLKIN AKILVSNLIS MAFLLLVAGY GFYQLNASIN ALQDIYENRI IPLKQMNIVS
     RDLMQIRVNM LTEMIALQEG DKAEIRRRID DTDRLKKEME EQLAAFEKTV LTEEEARRYA
     DYRSTEKAGA EIRGRFRDAI LRGQEEEASR LSVQWRDNYR QMRDHINRLV DIQSEVAQQL
     YDEEVTRFRI TIVVFTVIIA LSVVAALTIL TLMRRYISTP LQNAVDRVRD LAEGEGDLTK
     RLEVNSTDEV GDMAKWINQF IGNIHDIVKE MSSNTNDVKA SAGSLTGASQ NLSAGMEEMS
     VQSRNISAAA TQMNQNFQVI SSSVEELSTS VGEVARNASD ASKIAREADK TANETNQKIK
     QLGVDAQEIG KVVEAIQGIA SQTNLLALNA AIEAAGAGDA GKGFAVVASE VKELARQAAE
     ASDEIKTRIE AIQNSTEMAV ESISMITSVI SKINEFSTSI ASSVEEQSIT AKEIAGNVNQ
     SAQASSDVVQ NITGISTATQ DGAKNAQSLS GLATQLDTLS SRLGQIVSRF RI
//
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