ID E8TFX4_MESCW Unreviewed; 315 AA.
AC E8TFX4;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Surface presentation of antigens (SPOA) protein {ECO:0000313|EMBL:ADV11116.1};
GN OrderedLocusNames=Mesci_1963 {ECO:0000313|EMBL:ADV11116.1};
OS Mesorhizobium ciceri biovar biserrulae (strain HAMBI 2942 / LMG 23838 /
OS WSM1271).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=765698 {ECO:0000313|EMBL:ADV11116.1, ECO:0000313|Proteomes:UP000007471};
RN [1] {ECO:0000313|Proteomes:UP000007471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAMBI 2942 / LMG 23838 / WSM1271
RC {ECO:0000313|Proteomes:UP000007471};
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Nandasena K., Reeve W.G., Howieson J.G., O'Hara G.,
RA Tiwari R.P., Woyke T.;
RT "Complete sequence of chromosome of Mesorhizobium ciceri bv. biserrulae
RT WSM1271.";
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: FliM 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:ARBA00025044}.
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DR EMBL; CP002447; ADV11116.1; -; Genomic_DNA.
DR RefSeq; WP_013529804.1; NC_014923.1.
DR RefSeq; YP_004141166.1; NC_014923.1.
DR AlphaFoldDB; E8TFX4; -.
DR STRING; 765698.Mesci_1963; -.
DR KEGG; mci:Mesci_1963; -.
DR PATRIC; fig|765698.3.peg.2418; -.
DR eggNOG; COG1868; Bacteria.
DR HOGENOM; CLU_879623_0_0_5; -.
DR OrthoDB; 8273530at2; -.
DR Proteomes; UP000007471; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0097588; P:archaeal or bacterial-type flagellum-dependent cell motility; IEA:UniProtKB-KW.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1550.10; CheC-like; 1.
DR Gene3D; 2.30.330.10; SpoA-like; 1.
DR InterPro; IPR028976; CheC-like_sf.
DR InterPro; IPR001543; FliN-like_C.
DR InterPro; IPR036429; SpoA-like_sf.
DR PANTHER; PTHR30034; FLAGELLAR MOTOR SWITCH PROTEIN FLIM; 1.
DR PANTHER; PTHR30034:SF6; SURFACE PRESENTATION OF ANTIGENS PROTEIN SPAO; 1.
DR Pfam; PF01052; FliMN_C; 1.
DR SUPFAM; SSF101801; Surface presentation of antigens (SPOA); 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Flagellar rotation {ECO:0000256|ARBA:ARBA00022779};
KW Membrane {ECO:0000256|ARBA:ARBA00023136}.
FT DOMAIN 226..296
FT /note="Flagellar motor switch protein FliN-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01052"
SQ SEQUENCE 315 AA; 33349 MW; 345C3806C29F8233 CRC64;
MTSLGSPAEA RSLIIERLVG DSGEAAQVID AGRAMAERAV PLLQKTLTSE FGVPVVVDLK
AIEVSRVPEA RSRAGDTFAM TVIGSSASSD AMTLVIDAPA IAIMVCTLFG GDPDLPASPI
ERDLSQIEID VSTMVFQQVA QALNGSGKRS LDLRLPAPRA MSGTEAKRYV LRDGAAIRIV
LGISTPADSG TVTVTMPQRV VLASRDGAVP VSDDDHGPSW RARFSEEVMR STVALEATMP
LARLTLGDLA GFEIGDVIEF EETAQSQARL SARGKTLFVC EFGKLGQNYT VRIRQPYDAG
QDFIDGLMPA AAGRA
//
