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Database: UniProt
Entry: I3CF58_9GAMM
LinkDB: I3CF58_9GAMM
Original site: I3CF58_9GAMM 
ID   I3CF58_9GAMM            Unreviewed;       804 AA.
AC   I3CF58;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:EIJ42251.1};
GN   ORFNames=BegalDRAFT_1356 {ECO:0000313|EMBL:EIJ42251.1};
OS   Beggiatoa alba B18LD.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Thiotrichaceae; Beggiatoa.
OX   NCBI_TaxID=395493 {ECO:0000313|EMBL:EIJ42251.1, ECO:0000313|Proteomes:UP000005744};
RN   [1] {ECO:0000313|EMBL:EIJ42251.1, ECO:0000313|Proteomes:UP000005744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B18LD {ECO:0000313|EMBL:EIJ42251.1,
RC   ECO:0000313|Proteomes:UP000005744};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Held B., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Samuel K., Teske A.,
RA   Mueller J., Woyke T.;
RT   "Improved High-Quality Draft sequence of Beggiatoa alba B18lD.";
RL   Submitted (NOV-2011) 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; JH600070; EIJ42251.1; -; Genomic_DNA.
DR   RefSeq; WP_002685021.1; NZ_JH600070.1.
DR   AlphaFoldDB; I3CF58; -.
DR   STRING; 395493.BegalDRAFT_1356; -.
DR   eggNOG; COG0840; Bacteria.
DR   HOGENOM; CLU_000445_107_20_6; -.
DR   OrthoDB; 6433966at2; -.
DR   Proteomes; UP000005744; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProt.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   CDD; cd11386; MCP_signal; 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; IPR003660; HAMP_dom.
DR   InterPro; IPR024478; HlyB_4HB_MCP.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   PANTHER; PTHR43531:SF11; METHYL-ACCEPTING CHEMOTAXIS PROTEIN 3; 1.
DR   PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR   Pfam; PF12729; 4HB_MCP_1; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF18947; HAMP_2; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   SMART; SM00304; HAMP; 2.
DR   SMART; SM00283; MA; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR   PROSITE; PS50885; HAMP; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005744};
KW   Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        183..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          210..262
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          489..718
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
FT   REGION          777..804
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          247..274
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          707..734
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   804 AA;  90382 MW;  C3AF06086ECAEE67 CRC64;
     MKHLSIGKKF LILAIFSIAT IIGVGLYSLY NTATTFAWVD DVYNTAQDVQ DIALDIGEPL
     NKVHQLSLLI VTIPQQKEQF NLNIEQQAII KNLDEIIAKW QARDDIVKYQ TSFNQFQQAW
     TQYKTLSSYT IQTLLEGYRE AAFINASGAE QQQFDVLLFA FHQWMTEHIK NAKQIQVDAT
     KTYQLTLIVI IISFSLFILL VSFFNFYTAQ LIVKPINKAV AIANAIANGN LQNQITDITR
     DESGQLLQSL AQMQNQLREQ IAEEKRIADE AMRINQALDS VTTQVLITDN NYKIIYMNKA
     LKNFFQQEAD NFRRELPQFD PAQLLNNSID VLHKDASAHR ELLARLQTTE KSKLDLEGLT
     IEYMLTPVIN EQGERIGFVK EFNNRTQEVA TEQEIKQVIH AASQGDFKQR IQLTQKVGFF
     KAVSENINHI MDLNQQVLQD TMRMFAALAK GDLTQAITHN YIGDFAQLKT DANTTVMKLT
     SVMELIQASA QTIDETAETL LQNNLSLNQR TESQAAALEE TAASIEEMTS TIQQNANNAK
     QANDLAINAR KDAQAGGEIV AATIQAMTNI NQSSKRVADI IGVINDIAFQ TNLLALNAAV
     EAARAGEQGR GFAVVAGEVR NLAQRSAEAA KEIRLLIQDS VNKINEGSIL VNQSGEALQR
     IFTAVKKVSD IIADITDASQ EQTLGIHQVN KAISQMDEMT QQNNTMVTQA MEANETMREQ
     ASQLTQQVAF FQLKNTTKVV PNLTSNTQKT VKQLPQSPSK VTLPVFKHEN YKHLEKMQER
     QKSKTTQRQT QVTLKTHDDD WEDF
//
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