ID   FLGI_ALTMD              Reviewed;         370 AA.
AC   B4RV29; F2G366;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Flagellar P-ring protein {ECO:0000255|HAMAP-Rule:MF_00416};
DE   AltName: Full=Basal body P-ring protein {ECO:0000255|HAMAP-Rule:MF_00416};
DE   Flags: Precursor;
GN   Name=flgI {ECO:0000255|HAMAP-Rule:MF_00416};
GN   OrderedLocusNames=MADE_1005740;
OS   Alteromonas mediterranea (strain DSM 17117 / CIP 110805 / LMG 28347 / Deep
OS   ecotype).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX   NCBI_TaxID=1774373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17117 / CIP 110805 / LMG 28347 / Deep ecotype;
RX   PubMed=18670397; DOI=10.1038/ismej.2008.74;
RA   Ivars-Martinez E., Martin-Cuadrado A.-B., D'Auria G., Mira A., Ferriera S.,
RA   Johnson J., Friedman R., Rodriguez-Valera F.;
RT   "Comparative genomics of two ecotypes of the marine planktonic copiotroph
RT   Alteromonas macleodii suggests alternative lifestyles associated with
RT   different kinds of particulate organic matter.";
RL   ISME J. 2:1194-1212(2008).
CC   -!- FUNCTION: Assembles around the rod to form the L-ring and probably
CC       protects the motor/basal body from shearing forces during rotation.
CC       {ECO:0000255|HAMAP-Rule:MF_00416}.
CC   -!- SUBUNIT: The basal body constitutes a major portion of the flagellar
CC       organelle and consists of four rings (L,P,S, and M) mounted on a
CC       central rod. {ECO:0000255|HAMAP-Rule:MF_00416}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_00416}.
CC       Bacterial flagellum basal body {ECO:0000255|HAMAP-Rule:MF_00416}.
CC   -!- SIMILARITY: Belongs to the FlgI family. {ECO:0000255|HAMAP-
CC       Rule:MF_00416}.
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DR   EMBL; CP001103; AEA97290.1; -; Genomic_DNA.
DR   RefSeq; WP_012517633.1; NC_011138.3.
DR   AlphaFoldDB; B4RV29; -.
DR   SMR; B4RV29; -.
DR   EnsemblBacteria; AEA97290; AEA97290; MADE_1005740.
DR   KEGG; amc:MADE_1005740; -.
DR   HOGENOM; CLU_045235_1_0_6; -.
DR   OMA; FTEQSFR; -.
DR   Proteomes; UP000001870; Chromosome.
DR   GO; GO:0009428; C:bacterial-type flagellum basal body, distal rod, P ring; IEA:InterPro.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:InterPro.
DR   HAMAP; MF_00416; FlgI; 1.
DR   InterPro; IPR001782; Flag_FlgI.
DR   PANTHER; PTHR30381; PTHR30381; 1.
DR   Pfam; PF02119; FlgI; 1.
DR   PRINTS; PR01010; FLGPRINGFLGI.
PE   3: Inferred from homology;
KW   Bacterial flagellum; Periplasm; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00416"
FT   CHAIN           22..370
FT                   /note="Flagellar P-ring protein"
FT                   /id="PRO_1000123966"
SQ   SEQUENCE   370 AA;  38729 MW;  A3FA975845B74817 CRC64;
     MRLFSVVLAV FTLLLPSQAF AQRIKDVASI QGVRSNQLVG YGLVVGLPGT GEQSPFTEQS
     FRTMLRNFGI SLDANTKPKI RNVAAVAVHA DLPAFAKPGQ TIDITVSSVG EAASLQGGTL
     LQTFLRGVDG KVYAVAQGSL VVSGFGAQGG DGSRIVVNTP TVGRIPNGAM VEQSVPTGFA
     NGDTLTLNLH YPDFSTAKSL ADTINERLGA QPENGYVIAK PIDAASVRVS APRDVGQRVG
     FLATLENFEF TPADAPARVV INSRTGTIVI GSDVRLLPAA ITHGGLTVTI SENQQVTQPN
     AFADGQTAIT TQSIVDVDLA DSRMFKFEPG VTLDQLVRAV NEVGAAPGDL MAILEALRHA
     GALRGELVII