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Database: UniProt
Entry: A0A0T7BXB8_9CYAN
LinkDB: A0A0T7BXB8_9CYAN
Original site: A0A0T7BXB8_9CYAN 
ID   A0A0T7BXB8_9CYAN        Unreviewed;      1000 AA.
AC   A0A0T7BXB8;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Chemotaxis protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=IJ00_22880 {ECO:0000313|EMBL:AKG23758.1};
OS   Calothrix sp. 336/3.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC   Calothrix.
OX   NCBI_TaxID=1337936 {ECO:0000313|EMBL:AKG23758.1, ECO:0000313|Proteomes:UP000065745};
RN   [1] {ECO:0000313|EMBL:AKG23758.1, ECO:0000313|Proteomes:UP000065745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=336/3 {ECO:0000313|EMBL:AKG23758.1,
RC   ECO:0000313|Proteomes:UP000065745};
RX   PubMed=25614574;
RA   Isojarvi J., Shunmugam S., Sivonen K., Allahverdiyeva Y., Aro E.M.,
RA   Battchikova N.;
RT   "Draft genome sequence of calothrix strain 336/3, a novel h2-producing
RT   cyanobacterium isolated from a finnish lake.";
RL   Genome Announc. 3:0-0(2015).
CC   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000256|ARBA:ARBA00029447}.
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DR   EMBL; CP011382; AKG23758.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0T7BXB8; -.
DR   STRING; 1337936.IJ00_22880; -.
DR   KEGG; calh:IJ00_22880; -.
DR   eggNOG; COG0840; Bacteria.
DR   eggNOG; COG2203; Bacteria.
DR   eggNOG; COG5000; Bacteria.
DR   Proteomes; UP000065745; Chromosome.
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   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 6.10.340.10; -; 1.
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; PF00672; HAMP; 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; SSF158472; HAMP 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; 2.
DR   PROSITE; PS50046; PHYTOCHROME_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000065745};
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        395..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          418..470
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          494..630
FT                   /note="Phytochrome chromophore attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS50046"
FT   DOMAIN          663..714
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          719..955
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          780..817
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1000 AA;  111053 MW;  F0EB35EE75D7C33E CRC64;
     MNNKVNSDET QVQTSQPRKK YRGNIVRTNN RYDELALKIL TKTPVIPDET PEMKPSLWER
     FTNLPIGRKQ LIVLLASELL SIFVISSIGR LLITHNLDSL SLEQAKSEVM VSDINYNIKI
     NQMGFGFRGQ ADNAAIIKAA SIYNSGQTLN PEDKNQVKQI LQNEIQARKI EYATLVGKDL
     KIIVNANADR TGEIFNPDNL VQEVFNYPRQ IKVNSIVKSS EILREAPPLP NGVNRQDFLI
     RYTVTPVRDL QTRNVIGALV SGDIVNGKIP ITKATLKATG GGYSAIYLRK PTGELSLVTS
     LYQGASQNIN QAETDVALPP EGIALLRAAT VTDGKPVAGK LKIGQQTYAI AAKAVPNKII
     ETEDEQLSIF GDAPVGILVR GTPQTTLNQL LGQSFWLELL SVYIAVIIIL MGAYVLRRSI
     ITPIQNLRLK AQSFATGDRT VRADVFAIDE IGQIAVSFNA MADSIVSQSH SQQNESYLTQ
     LVNEINIRCR SSLNTQYILN TAVNRIRDAL KTDRVIVYQF NPSWEGRVVA ESVAVEFPVA
     IGAEINDSCF TQKSIHKYQQ GTVLNIDNVE TANLTECHLN LLKRFGIKAN LVAPIVINNQ
     LYGLLIAHQC STPRNWQEVE INFLKQVAVP IAYALEKAAL QEQIQQVSSQ VESISQEKSL
     QQATIYQQIE KILQDIEHLS QGDLTVQTDV IPGEMSFVGE YINNTISNLR AIATKIQVSA
     QQVNSAIVDN DTAMSQFADT NLQQSAEIKQ TLSHVEQFTV NLKDLLESTQ QSATESYTIV
     DAAQENEVAI EMNLQNLRNL RTNIDDMAKK IKRLGESSQQ LSRIIFLINQ IAMQSNLLAV
     NAGLEIAREG KEEQNFAIVA EEVGELATHC TEATQEIEKI IENIQKDAQL TIKSMESGTI
     QVIESSHNLE ITKQKLNQML QVSQQVHELV QNISQSTTYK LTISEDLINA IENISHALDV
     NSHLSQEISQ SLNQTVDISQ ELQESVAGFK TYLTLPQKYN
//
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