ID E7NVY6_TREPH Unreviewed; 411 AA.
AC E7NVY6;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=HAMP domain protein {ECO:0000313|EMBL:EFW37239.1};
GN ORFNames=HMPREF9554_02249 {ECO:0000313|EMBL:EFW37239.1};
OS Treponema phagedenis F0421.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=754027 {ECO:0000313|EMBL:EFW37239.1, ECO:0000313|Proteomes:UP000004157};
RN [1] {ECO:0000313|EMBL:EFW37239.1, ECO:0000313|Proteomes:UP000004157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0421 {ECO:0000313|EMBL:EFW37239.1,
RC ECO:0000313|Proteomes:UP000004157};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFW37239.1}.
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DR EMBL; AEFH01000193; EFW37239.1; -; Genomic_DNA.
DR RefSeq; WP_002699746.1; NZ_GL638090.1.
DR AlphaFoldDB; E7NVY6; -.
DR STRING; 162.TPHV1_30039; -.
DR eggNOG; COG0840; Bacteria.
DR HOGENOM; CLU_000445_107_18_12; -.
DR Proteomes; UP000004157; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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; 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; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR PANTHER; PTHR32089:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 1.
DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 2.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 3: Inferred from homology;
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW ProRule:PRU00284}.
FT DOMAIN 24..78
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 125..347
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 411 AA; 44779 MW; E3773122CF52BD00 CRC64;
MLITAVGLII SSALIIVSSF IFAGTLIKPI NKVTLALKNI SEGAGDLTVR LKSKRRDEVG
MLCEYFNQTM QKIQESIISI SRQTAVMNET SITLSTNMNE SASSVQQINT NISGIKEKVQ
TILQDSDRTG ANVQAVVAGM QNLNTTMHSQ TKEVETTLNS LQGIVSNISF VTEILDTNID
SVQSLQEETE EGKQSVERSA VLTKQINEES EGLLEASSVI QHIASQTNLL AMNAAIEAAH
AGDAGKGFAV VADEIRKLAE ESSTQGKSIT RVLKELKTTI EEVSKQSLLV QNKFDSIFNL
TKVVRSQEDQ IMKAMNMQAK SGENISQAME SINRLLAGIT TQSAEMHQYG ESITEELKIL
QHGIYLINDN ITEISAGTEQ VFAAIVDVNI QAKLNEESVQ NVTKAIHSFK V
//
