ID F2JTV6_MARM1 Unreviewed; 961 AA.
AC F2JTV6;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Methyl-accepting chemotaxis sensory transducer {ECO:0000313|EMBL:ADZ90377.1};
GN OrderedLocusNames=Marme_1102 {ECO:0000313|EMBL:ADZ90377.1};
OS Marinomonas mediterranea (strain ATCC 700492 / JCM 21426 / NBRC 103028 /
OS MMB-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=717774 {ECO:0000313|EMBL:ADZ90377.1, ECO:0000313|Proteomes:UP000001062};
RN [1] {ECO:0000313|EMBL:ADZ90377.1, ECO:0000313|Proteomes:UP000001062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1
RC {ECO:0000313|Proteomes:UP000001062};
RX PubMed=22675599; DOI=10.4056/sigs.2545743;
RA Lucas-Elio P., Goodwin L., Woyke T., Pitluck S., Nolan M., Kyrpides N.C.,
RA Detter J.C., Copeland A., Teshima H., Bruce D., Detter C., Tapia R.,
RA Han S., Land M.L., Ivanova N., Mikhailova N., Johnston A.W.,
RA Sanchez-Amat A.;
RT "Complete genome sequence of the melanogenic marine bacterium Marinomonas
RT mediterranea type strain (MMB-1(T)).";
RL Stand. Genomic Sci. 6:63-73(2012).
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
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DR EMBL; CP002583; ADZ90377.1; -; Genomic_DNA.
DR RefSeq; WP_013660282.1; NZ_CP047696.1.
DR AlphaFoldDB; F2JTV6; -.
DR STRING; 717774.Marme_1102; -.
DR KEGG; mme:Marme_1102; -.
DR PATRIC; fig|717774.3.peg.1143; -.
DR eggNOG; COG0840; Bacteria.
DR HOGENOM; CLU_000445_107_20_6; -.
DR OrthoDB; 9765776at2; -.
DR Proteomes; UP000001062; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 1.
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; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR PANTHER; PTHR43531:SF14; METHYL-ACCEPTING CHEMOTAXIS PROTEIN I-RELATED; 1.
DR PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF18947; HAMP_2; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
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 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:UP000001062};
KW Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 13..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 341..393
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 626..855
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT REGION 641..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 867..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 826..864
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 887..919
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..950
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 961 AA; 103925 MW; E525C9F68E5FB542 CRC64;
MQWMNNIKLS RKFVLLGILV AISVGVPIKF LIEREMLIFE KANSEILGVE PTNMLLEYVK
LLQQHRGKSA IFLNDVSRSS ADIDQLGQKI DAFHVTVLQE MKTQFPNSPI VTDVEHLKVN
FDQLRSEVRS RAVTPSESFS SHTGLVMQAV AEDIPFVLEY SGLMFDSSKE TAYLTTASKL
NLPLSIEGIA RLRGFGSGAL ASDYVTQEQI GKVISALAFI EAPHIELLHN LKAAYDSTGD
PRANELYREA KVIDEDYQAL LDIAQTYVMV EGVPNYSAES FFDNATVVID ELFLLSRHSS
DLMKELLLER VEHVKVELAT SLGIVFGFLI LAVVASVFIL RNLNVALSSL SEAARSVANG
DYEVALNNTR KDEFGLLNQS VVDMSESLHQ GELEREANLK EIADRLVETT RVEQALNAAG
TNVVIVSTER KVIYANTSMK KMLKNAELSL RDVISGFDAS AIVGQSIDVF NVSGQQTILP
ETLNSPYESN LELAGMHFRV FANPIFSQEN ERIGSVVEWL DLTSEVEAQN EIGSIVGEAA
RGNFTVRAKE EGKHEFMLFM AQSLNKLMTT ADEGLSDVTR VLMALSNGNL TEKITQEYEG
QFNDLKTYCN QTSENLASMI GELRFAAETI NVAASEIAQG NSDLSNRTET QASSLEETAS
SMEEITSTVR RNADNASEAN TLASEAAGVA ITGGDLIHQV VETMTAINES SQKISDIIGV
IDGIAFQTNI LALNAAVEAA RAGEQGRGFA VVASEVRTLA QRSANAAKDI KALISDSVSK
IADGNELVGQ SGETMGQIVD SIKRVNSIMT EIAAASTQQA AGVDEINRTI SQMDEMTQQN
AALVEEAAAS AESMRSQANG LERQVSNFTL DSNAESNERV SFAGDEATRK ASSSTPARHL
SSSNSHNASQ STSNAPRVVA TAPNKGAKAA MPSPKAHTST SGSSAAITAG GSISEDDWEE
F
//