FLIF_RHIME
ID FLIF_RHIME Reviewed; 557 AA.
AC O54239;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 24-OCT-2001, sequence version 2.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Flagellar M-ring protein;
GN Name=fliF; OrderedLocusNames=R00646; ORFNames=SMc03014;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=RU11/001;
RX PubMed=9858749; DOI=10.1016/s0378-1119(98)00160-7;
RA Sourjik V., Sterr W., Platzer J., Bos I., Haslbeck M., Schmitt R.;
RT "Mapping of 41 chemotaxis, flagellar and motility genes to a single region
RT of the Sinorhizobium meliloti chromosome.";
RL Gene 223:283-290(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
CC -!- FUNCTION: The M ring may be actively involved in energy transduction.
CC {ECO:0000250}.
CC -!- SUBUNIT: The basal body constitutes a major portion of the flagellar
CC organelle and consists of five rings (E,L,P,S, and M) mounted on a
CC central rod. The M ring is integral to the inner membrane of the cell
CC and may be connected to the flagellar rod via the S ring. The S
CC (supramembrane ring) lies just distal to the M ring. The L and P rings
CC lie in the outer membrane and the periplasmic space, respectively (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Bacterial flagellum basal body
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FliF family. {ECO:0000305}.
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DR EMBL; AJ224445; CAA11947.1; -; Genomic_DNA.
DR EMBL; AL591688; CAC45218.1; -; Genomic_DNA.
DR RefSeq; NP_384752.1; NC_003047.1.
DR RefSeq; WP_010968722.1; NC_003047.1.
DR AlphaFoldDB; O54239; -.
DR SMR; O54239; -.
DR STRING; 266834.SMc03014; -.
DR EnsemblBacteria; CAC45218; CAC45218; SMc03014.
DR GeneID; 61602113; -.
DR KEGG; sme:SMc03014; -.
DR PATRIC; fig|266834.11.peg.2019; -.
DR eggNOG; COG1766; Bacteria.
DR HOGENOM; CLU_028108_4_0_5; -.
DR OMA; ITTRPHY; -.
DR Proteomes; UP000001976; Chromosome.
DR GO; GO:0009431; C:bacterial-type flagellum basal body, MS ring; IEA:InterPro.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 Gene3D; 3.30.300.30; -; 1.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR013556; Flag_M-ring_C.
DR InterPro; IPR000067; FlgMring_FliF.
DR InterPro; IPR006182; FliF_N_dom.
DR InterPro; IPR043427; YscJ/FliF.
DR PANTHER; PTHR30046; PTHR30046; 1.
DR PANTHER; PTHR30046:SF0; PTHR30046:SF0; 1.
DR Pfam; PF01514; YscJ_FliF; 1.
DR Pfam; PF08345; YscJ_FliF_C; 1.
DR PIRSF; PIRSF004862; FliF; 1.
DR PRINTS; PR01009; FLGMRINGFLIF.
DR TIGRFAMs; TIGR00206; fliF; 1.
PE 3: Inferred from homology;
KW Bacterial flagellum; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..557
FT /note="Flagellar M-ring protein"
FT /id="PRO_0000180885"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 279..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 46
FT /note="P -> R (in Ref. 1; CAA11947)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="A -> G (in Ref. 1; CAA11947)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 557 AA; 59090 MW; CAA139C08D68570E CRC64;
MNLFDQFSTF TKNLSNLGQG KLIALAVAGV VAIGFVLGAG IYVNRPSFET LYVGLERSDV
TQISIALAEA NVDFEVGTDG GSIQVPVGMT GKARLLLAER GLPSSANAGY ELFDNVGSLG
LTSFMQEVTR VRALEGEIAR TIQQISGIAA ARVHIVMPER GSFRKAEQTP TASVMIRASA
TVGRSAASSI RHLVASSVPG LDVDDVTVLD STGQLLASGD DPSNSALNQS LGVVQNVQSD
LEKKIDNALA PFLGMDNFRT SVTARLNTDA QQIQETVFDP ESRVERSTRV IKEEQKSSQQ
QPDNAATVQQ NVPQAAPRGG AGQQSSDEAE KKEEQTNYEI NSKTIATVKN SYSIERLSIA
VVVNRGRLAA MAGEPADQAK IDAYLQEMQK IVSSAAGIDP GRGDVVTLNA MDFVETQLLD
QAVPGPGIME MLTRNLGGII NALAFVAVAF LVVWFGMRPL ARQLGFGGQA GKLEGEAAGL
ELPDFSPAGA GAGGALMEGF GSDFGFDGGD DLLNLGDEAG FNRRVKEGPE RRLARMVEIS
EERAAKILRK WAVDRAA
