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Database: UniProt
Entry: A0L4A4_MAGMM
LinkDB: A0L4A4_MAGMM
Original site: A0L4A4_MAGMM 
ID   A0L4A4_MAGMM            Unreviewed;       336 AA.
AC   A0L4A4;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=Flagellar motor switch protein FliG {ECO:0000256|ARBA:ARBA00021870, ECO:0000256|PIRNR:PIRNR003161};
GN   OrderedLocusNames=Mmc1_0270 {ECO:0000313|EMBL:ABK42797.1};
OS   Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Magnetococcales;
OC   Magnetococcaceae; Magnetococcus.
OX   NCBI_TaxID=156889 {ECO:0000313|EMBL:ABK42797.1, ECO:0000313|Proteomes:UP000002586};
RN   [1] {ECO:0000313|Proteomes:UP000002586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1
RC   {ECO:0000313|Proteomes:UP000002586};
RX   PubMed=19465526; DOI=10.1128/AEM.02874-08;
RA   Schubbe S., Williams T.J., Xie G., Kiss H.E., Brettin T.S., Martinez D.,
RA   Ross C.A., Schuler D., Cox B.L., Nealson K.H., Bazylinski D.A.;
RT   "Complete genome sequence of the chemolithoautotrophic marine magnetotactic
RT   coccus strain MC-1.";
RL   Appl. Environ. Microbiol. 75:4835-4852(2009).
RN   [2] {ECO:0000313|EMBL:ABK42797.1, ECO:0000313|Proteomes:UP000002586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1
RC   {ECO:0000313|Proteomes:UP000002586};
RX   PubMed=22581902;
RA   Bazylinski D.A., Williams T.J., Lefevre C.T., Berg R.J., Zhang C.L.,
RA   Bowser S.S., Dean A.J., Beveridge T.J.;
RT   "Magnetococcus marinus gen. nov., sp. nov., a marine, magnetotactic
RT   bacterium that represents a novel lineage (Magnetococcaceae fam. nov.;
RT   Magnetococcales ord. nov.) at the base of the Alphaproteobacteria.";
RL   Int. J. Syst. Evol. Microbiol. 0:0-0(2012).
CC   -!- FUNCTION: FliG is one of three proteins (FliG, FliN, FliM) that forms
CC       the rotor-mounted switch complex (C ring), located at the base of the
CC       basal body. This complex interacts with the CheY and CheZ chemotaxis
CC       proteins, in addition to contacting components of the motor that
CC       determine the direction of flagellar rotation.
CC       {ECO:0000256|ARBA:ARBA00025598, ECO:0000256|PIRNR:PIRNR003161}.
CC   -!- SUBCELLULAR LOCATION: Bacterial flagellum basal body
CC       {ECO:0000256|ARBA:ARBA00004117, ECO:0000256|PIRNR:PIRNR003161}. Cell
CC       inner membrane {ECO:0000256|PIRNR:PIRNR003161}; Peripheral membrane
CC       protein {ECO:0000256|PIRNR:PIRNR003161}; Cytoplasmic side
CC       {ECO:0000256|PIRNR:PIRNR003161}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004287}.
CC   -!- SIMILARITY: Belongs to the FliG family. {ECO:0000256|ARBA:ARBA00010299,
CC       ECO:0000256|PIRNR:PIRNR003161}.
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DR   EMBL; CP000471; ABK42797.1; -; Genomic_DNA.
DR   RefSeq; WP_011711969.1; NC_008576.1.
DR   AlphaFoldDB; A0L4A4; -.
DR   STRING; 156889.Mmc1_0270; -.
DR   KEGG; mgm:Mmc1_0270; -.
DR   eggNOG; COG1536; Bacteria.
DR   HOGENOM; CLU_047835_1_1_5; -.
DR   OrthoDB; 9780302at2; -.
DR   Proteomes; UP000002586; Chromosome.
DR   GO; GO:0009425; C:bacterial-type flagellum basal body; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR   GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.220.30; -; 3.
DR   InterPro; IPR000090; Flg_Motor_Flig.
DR   InterPro; IPR023087; Flg_Motor_Flig_C.
DR   InterPro; IPR011002; FliG_a-hlx.
DR   InterPro; IPR032779; FliG_M.
DR   InterPro; IPR028263; FliG_N.
DR   NCBIfam; TIGR00207; fliG; 1.
DR   PANTHER; PTHR30534; FLAGELLAR MOTOR SWITCH PROTEIN FLIG; 1.
DR   PANTHER; PTHR30534:SF0; FLAGELLAR MOTOR SWITCH PROTEIN FLIG; 1.
DR   Pfam; PF01706; FliG_C; 1.
DR   Pfam; PF14841; FliG_M; 1.
DR   Pfam; PF14842; FliG_N; 1.
DR   PIRSF; PIRSF003161; FliG; 1.
DR   PRINTS; PR00954; FLGMOTORFLIG.
DR   SUPFAM; SSF48029; FliG; 2.
PE   3: Inferred from homology;
KW   Bacterial flagellum {ECO:0000256|ARBA:ARBA00023143,
KW   ECO:0000256|PIRNR:PIRNR003161};
KW   Cell inner membrane {ECO:0000256|PIRNR:PIRNR003161};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|PIRNR:PIRNR003161};
KW   Cell projection {ECO:0000313|EMBL:ABK42797.1};
KW   Chemotaxis {ECO:0000256|ARBA:ARBA00022500, ECO:0000256|PIRNR:PIRNR003161};
KW   Cilium {ECO:0000313|EMBL:ABK42797.1};
KW   Flagellar rotation {ECO:0000256|ARBA:ARBA00022779,
KW   ECO:0000256|PIRNR:PIRNR003161}; Flagellum {ECO:0000313|EMBL:ABK42797.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR003161};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002586}.
FT   DOMAIN          2..105
FT                   /note="Flagellar motor switch protein FliG N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14842"
FT   DOMAIN          113..187
FT                   /note="Flagellar motor switch protein FliG middle"
FT                   /evidence="ECO:0000259|Pfam:PF14841"
FT   DOMAIN          221..326
FT                   /note="Flagellar motor switch protein FliG C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01706"
SQ   SEQUENCE   336 AA;  37622 MW;  8088DAC87C64D750 CRC64;
     MKLTGKEKAA VFILSLPDDD AKKIMEGMSE DEIREISRTI ARLGQMDEET VKAVREEFLS
     LFENQSFNVR GGMQKVKDLI FKVLGKEKGR HLLKELQQGP KNTPWEILNE MEPTLVATFL
     ANEHPQSIAL IISQLNAEQA SFIIDYLAPE VQQEVIYRMA KLGNLPPGAL EDIEESLLAE
     LEAMGASRGL YTSEGGGGVK KVAELLNLMP RDTSDKLLAF LDEEDNPLAE DVRKEMFLFE
     DLLLMDDKSF QTLLREVSND ELLTALKGTD DRLKEKFFTN MSERAAEMLR EDLEMMGPVK
     VSDVEQAQQA ILKVARQLEA DGAIVIMGKG SDDVVL
//
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