ID A0A1Z4NGS0_9CYAN Unreviewed; 1066 AA.
AC A0A1Z4NGS0;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Methyl accepting chemotaxis protein {ECO:0000313|EMBL:BAZ04920.1};
GN ORFNames=NIES3974_15660 {ECO:0000313|EMBL:BAZ04920.1};
OS Calothrix sp. NIES-3974.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=2005462 {ECO:0000313|EMBL:BAZ04920.1, ECO:0000313|Proteomes:UP000218621};
RN [1] {ECO:0000313|EMBL:BAZ04920.1, ECO:0000313|Proteomes:UP000218621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-3974 {ECO:0000313|EMBL:BAZ04920.1,
RC ECO:0000313|Proteomes:UP000218621};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-2017) 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}.
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DR EMBL; AP018254; BAZ04920.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4NGS0; -.
DR OrthoDB; 419276at2; -.
DR Proteomes; UP000218621; Chromosome.
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; cd18773; PDC1_HK_sensor; 1.
DR Gene3D; 3.30.450.40; -; 2.
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; 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; PF02743; dCache_1; 1.
DR Pfam; PF01590; GAF; 2.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00304; HAMP; 2.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF55781; GAF domain-like; 2.
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; 2.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000218621};
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 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 299..318
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 319..371
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 395..447
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 568..703
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 736..787
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 792..1029
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT COILED 352..386
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1066 AA; 118436 MW; 97E605068547F2B6 CRC64;
MQTTFSRSPL GLGLKKKAAI YSVIFSVIPV VIIGANTYGM MNQFIRRDIT LNKQLQAEGL
ASGINQFLLN RQLELELLAN QDFLNNDNNK LTQEEKELRL KNWLEKEKFY NSLVVLDLQG
NVKLKTSSQA TTPAKNADYL PKIRQSGSFT ISQPVLDNNR QNSRIYLNVP VKDRVTGEVI
RVIRGEISSQ KLLSGIGQKR LSQYLDSRKY YLLDQSGLVF LTNDSNQQGK PIGEIFAEWD
RLNNSPQMIT ETLPIVGNQK QALVTVVPTV TSADLGWRLV LSQDPNTAFA VSRNLLRNLF
ISSILTILLA VIIAVILARR LSSRLITANI AVTSLAQGNL DTRMPLAGGD ELTSLGANIN
EMAAQLQRLI RERSQETEQL KQFSQALLTI QQTATREELF KTITQEMMTA LGVERVTIYA
CNPDGSYTAI AESVVSGVKS LQQFPVSQDI MDNTRVLAVG DVNLAGYSND LRQQLQKMQV
KSRVVTPIVE DKQSTDGKRN RYRISALGVV PVAIAVDMCT RQRDWSSQEI DFIRQSAAQL
GVALERIDSQ TATQALKNLA VHLSSSWQSD DIYSLAVQDI RQALQVDRVV IYQFDPSYRG
KFLAESVVAG FPCAMGFKLT DTCLEEYVEK YRRGRVVAIN DIYDAGLSQC YIQQLETFAV
KANLVAPIIV GDELLGLLIA HQCSQGRIWQ IGEIDLFEQF ARMVGLALER ANLLQNTMTA
RDIAESIAQQ RSEETERMQT EILTLIDSIE KAIAGDLTVR AEVGVGEIGT IADFFNAIIE
SLRILVINVK NTATQVNQAI NDNAIAIKNV ALGACEQAKD TRKILETITA MRAKVKTTSE
TIAGMAQITS AIMQIAREND GKLQQAIADI GNLGEELEQN RHQTENLSES VQQIQRLING
INQSAMQTNL LAINTGIEVN RSGENNPANF TILLQEIANL ANRCTYVTHE IDTIVQNMHQ
DSSLLKEMME SGINQVNQSS KNIEISQTNL QQIVQICQQV DELMQSIATS IVETEQYSHQ
VSQKIHSMVE VSGNTSTTAQ EIADALEQTV QLSEELQHNI CNFQVD
//
