ID B4VNS7_9CYAN Unreviewed; 704 AA.
AC B4VNS7;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Methyl-accepting chemotaxis protein signaling domain {ECO:0000313|EMBL:EDX76543.1};
GN ORFNames=MC7420_4799 {ECO:0000313|EMBL:EDX76543.1};
OS Coleofasciculus chthonoplastes PCC 7420.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC Coleofasciculaceae; Coleofasciculus.
OX NCBI_TaxID=118168 {ECO:0000313|EMBL:EDX76543.1, ECO:0000313|Proteomes:UP000003835};
RN [1] {ECO:0000313|EMBL:EDX76543.1, ECO:0000313|Proteomes:UP000003835}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7420 {ECO:0000313|EMBL:EDX76543.1,
RC ECO:0000313|Proteomes:UP000003835};
RA Tandeau de Marsac N., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUL-2008) 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; DS989846; EDX76543.1; -; Genomic_DNA.
DR RefSeq; WP_006100271.1; NZ_DS989846.1.
DR AlphaFoldDB; B4VNS7; -.
DR STRING; 118168.MC7420_4799; -.
DR eggNOG; COG0840; Bacteria.
DR HOGENOM; CLU_391681_0_0_3; -.
DR OrthoDB; 9790669at2; -.
DR Proteomes; UP000003835; 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; 3.
DR Gene3D; 1.20.120.1530; -; 4.
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 InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR32089:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 1.
DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR Pfam; PF00672; HAMP; 3.
DR Pfam; PF18947; HAMP_2; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00304; HAMP; 4.
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; 4.
DR PROSITE; PS50192; T_SNARE; 1.
PE 3: Inferred from homology;
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Reference proteome {ECO:0000313|Proteomes:UP000003835};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW ProRule:PRU00284}.
FT DOMAIN 64..114
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 154..211
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 251..303
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 343..395
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 460..675
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT DOMAIN 605..667
FT /note="T-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50192"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 704 AA; 75173 MW; A42C7266E408D26F CRC64;
MTNNKLVKNR KPGRAVFFED PEGVENQETE KTVITESNHL SGNEPDPVDL PSEPLKSETS
LETELSSKSL QELKKALAAV RDGDFSVRLS AENGFGELAT IFNQMVTVNQ TFTTELVDMG
KTVAQEGKVS KQYSRPELQG SWRTNVDTVN EIINSLVNPT IEIARVLHAV AKGDLSQKIA
LEIEGKPLKG LFRRISTTVN KMVDQLDTFA VEVTQVARDV GIEGKLGGQA EVPGVSGIWK
ELTDNVNLMA KNLTDQVRSI TTVATAISEG NFSEKITVEA QGEILALKDT LNQMVDRLHT
IVIEITQVSQ DVGIEGKLGG QATVDGLSGS WRSLTQTVNF MAAHLTEQVR NIAAVSTAVA
QGDLSQKITV EAKGEILALK TTLNRMVDQL NTFAHEVTRL TQDVVNGKLG GQAMVEGVDG
TWKELTDNVN LMASNLTDQV KQIAQVAIAL SNASEHLTLE SQTMGATAEE TSVQAATVSS
AAEQVSTNTQ SVAIGMEQMH ASIKEIAKSA AEATTVATSA VTTAETTNQT IAQLGVSSTE
IGKIVKLITS IAQQTNLLAL NATIEAARAG EAGKGFAVVA NEVKELAKQT ANATEDISQK
VEAIQGDTKH SVDAIAQITT IIHQINDFQT TIASAVEEQT ATTNEIARNI NQVSLGSQEI
ARNITGVADA AQNTAQSASN TQNSALELSK TANELEQLVG QFKY
//
