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Database: UniProt
Entry: E7NXZ0_TREPH
LinkDB: E7NXZ0_TREPH
Original site: E7NXZ0_TREPH 
ID   E7NXZ0_TREPH            Unreviewed;       703 AA.
AC   E7NXZ0;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=HAMP domain protein {ECO:0000313|EMBL:EFW36554.1};
GN   ORFNames=HMPREF9554_02960 {ECO:0000313|EMBL:EFW36554.1};
OS   Treponema phagedenis F0421.
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC   Treponema.
OX   NCBI_TaxID=754027 {ECO:0000313|EMBL:EFW36554.1, ECO:0000313|Proteomes:UP000004157};
RN   [1] {ECO:0000313|EMBL:EFW36554.1, ECO:0000313|Proteomes:UP000004157}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0421 {ECO:0000313|EMBL:EFW36554.1,
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   -!- 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}.
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:EFW36554.1}.
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DR   EMBL; AEFH01000250; EFW36554.1; -; Genomic_DNA.
DR   RefSeq; WP_002701171.1; NZ_GL638118.1.
DR   AlphaFoldDB; E7NXZ0; -.
DR   STRING; 162.TPHV1_500001; -.
DR   eggNOG; COG0840; Bacteria.
DR   HOGENOM; CLU_000445_107_19_12; -.
DR   Proteomes; UP000004157; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   CDD; cd06225; HAMP; 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; 1.
DR   InterPro; IPR033479; dCache_1.
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; PF02743; dCache_1; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF00015; MCPsignal; 1.
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   Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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        15..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        292..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          316..370
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          417..639
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
SQ   SEQUENCE   703 AA;  76949 MW;  10D6B8D050CF808A CRC64;
     MGRAEKRKHS ITIKLVFYFG IVLLFSIALI SAVFLLTSYK ALTDNVTERL TLQAYNLSEI
     VNVNLQSLYR QLETIARNET VRDPNFNVSE KAHSLRYEAV KNTKNFITKL FILDTSGKGF
     QTDGTAVNHS GKIGVTTVLN GGMFISQPEP SAAGGFVSMY YYIPVYNVSQ KIINILVAEI
     NAAMLSRDIK NASIGKTGEA FIVGTDGTII AGKDEQIVKE KLNVLEKAKQ DNAYKDFDRF
     IQQALQYYGY NYDTYDFAGK KISGAFSKIS TTGWTLVICA PTEEFMGGVH KFMISVCVVI
     IITIVCAGFV ILVIAYQIAK PLQKTAMALK NISQGEGDLT ISLPVRGNDE ISDIALYFNE
     TIKKIRNSIA TVTYNIDKME AIGSELTEHA SKTELAAKKI EESIGNVKND VLSQTTGITE
     VASVMEQSVR TVEQLNKHIA TQAASVEQSS ASIEQMVTNI RAVTDILEEN TETVESLNES
     TDIGHTSLMH SVEITKMIIE RSDGLLEAST IIQNIASQTN LLAMNAAIEA AHAGNEGKGF
     AVVAAEIRKL AEEAARQSKS ITMVLKELKA MIGELGKSSD TVQSVFSDIY QFAETVKTQE
     DVIMKTMQMQ SAGGMEILRA IKSINTATTE VEHGATEMLT GSKETSTEMQ KLASIAAMIT
     ENMNTMNTDT IKINSAIIGI AEISRKTHQS IESLAEEVKK FKI
//
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