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Database: UniProt
Entry: A0A139WV14_9CYAN
LinkDB: A0A139WV14_9CYAN
Original site: A0A139WV14_9CYAN 
ID   A0A139WV14_9CYAN        Unreviewed;       788 AA.
AC   A0A139WV14;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Chemotaxis protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=WA1_41925 {ECO:0000313|EMBL:KYC36285.1};
OS   Scytonema hofmannii PCC 7110.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Scytonemataceae;
OC   Scytonema.
OX   NCBI_TaxID=128403 {ECO:0000313|EMBL:KYC36285.1, ECO:0000313|Proteomes:UP000076925};
RN   [1] {ECO:0000313|EMBL:KYC36285.1, ECO:0000313|Proteomes:UP000076925}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7110 {ECO:0000313|EMBL:KYC36285.1,
RC   ECO:0000313|Proteomes:UP000076925};
RX   PubMed=23221676; DOI=10.1093/gbe/evs117;
RA   Dagan T., Roettger M., Stucken K., Landan G., Koch R., Major P.,
RA   Gould S.B., Goremykin V.V., Rippka R., Tandeau de Marsac N., Gugger M.,
RA   Lockhart P.J., Allen J.F., Brune I., Maus I., Puhler A., Martin W.F.;
RT   "Genomes of Stigonematalean cyanobacteria (subsection V) and the evolution
RT   of oxygenic photosynthesis from prokaryotes to plastids.";
RL   Genome Biol. Evol. 5:31-44(2013).
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:KYC36285.1}.
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DR   EMBL; ANNX02000047; KYC36285.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139WV14; -.
DR   STRING; 128403.WA1_41925; -.
DR   Proteomes; UP000076925; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd11386; MCP_signal; 1.
DR   Gene3D; 3.30.450.40; -; 2.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   InterPro; IPR016132; Phyto_chromo_attachment.
DR   PANTHER; PTHR32089:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 1.
DR   PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00304; HAMP; 2.
DR   SMART; SM00283; MA; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 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; PS50046; PHYTOCHROME_2; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076925};
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        189..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          294..430
FT                   /note="Phytochrome chromophore attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS50046"
FT   DOMAIN          456..507
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          512..748
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
SQ   SEQUENCE   788 AA;  87251 MW;  777937E9A4A41DC8 CRC64;
     MSYQFHRDSQ AFYQKSYPRE ENTTLHQLMT TRKNHITAIF RLRDHMEWGG RPRRTSHSVR
     AGTPVPQEQS VVLDLENCCN RRFGVRLLRT LSLKTKATVA TAISTLSLLA IGTEAYPLAH
     LSTSQEINQA EQTNASAKAD YDNHVLKSNN RYQLVSDPAW KTPNGLPSFN REVAVAVKGK
     TALAPQQDLL LSLVIRIVLT ALVAIASAAF LYKWGITPIL NKTNEEEKLG QRELDTDIER
     GEDVAELGSK VNLMADQLKV LVREQVEQSR RLEAEAKRTQ IFTEITLHIR QFLNQKDLLQ
     ATADAIRNSL ATERVVVYRF HEDCSGTAIA ESVAADFPRM IERQIDDPCF RERYVQQYKN
     GRVRAIDNIY QANLTDCHIK TLEQFTVKAN LVAPILQEKQ LVGLLIAHQC SQPRTWQKWE
     INLFAQLAIQ VGFALDQAAL LEQLEIISQE QRQQKEVLQQ KLVELVSSIE AVSEGDLTVR
     AEVTAGEIGI IADFFNFIIK NLRQIVMTVK KAASEVNLAV GENSDAVQQL AFEALKQTEQ
     MTRALEDVNQ MTLSIQAVAD SAHQAKAVAR SAFDIARASA EAMGSTVSSI LNLQQTVTET
     ANKVNCLSEF SQEISVVVSL INKIAVQTNL LSINASLEMA RAGDEGRGFV VVVEEIGDLA
     AQSAQATTEI QQILEKIQLG TSDAVQAMSM GSTQVVEGAN LVKNAKLSLE QILDLSRQID
     QLVQSISSAT VSQAQTSGAV TILMQETANV SQRTSDSFDM VSGSLETTLE IAQQLQKSVS
     VFKTSEQN
//
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