(data stored in SCRATCH9089 zone)

SWISSPROT: FLGH_BURP1

ID   FLGH_BURP1              Reviewed;         222 AA.
AC   Q3JX21;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   11-DEC-2019, entry version 70.
DE   RecName: Full=Flagellar L-ring protein {ECO:0000255|HAMAP-Rule:MF_00415};
DE   AltName: Full=Basal body L-ring protein {ECO:0000255|HAMAP-Rule:MF_00415};
DE   Flags: Precursor;
GN   Name=flgH {ECO:0000255|HAMAP-Rule:MF_00415};
GN   OrderedLocusNames=BURPS1710b_0468;
OS   Burkholderia pseudomallei (strain 1710b).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320372;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1710b;
RA   Woods D.E., Nierman W.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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_00415}.
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_00415}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00415}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_00415}.
CC       Bacterial flagellum basal body {ECO:0000255|HAMAP-Rule:MF_00415}.
CC   -!- SIMILARITY: Belongs to the FlgH family. {ECO:0000255|HAMAP-
CC       Rule:MF_00415}.
DR   EMBL; CP000124; ABA49653.1; -; Genomic_DNA.
DR   EnsemblBacteria; ABA49653; ABA49653; BURPS1710b_0468.
DR   KEGG; bpm:BURPS1710b_0468; -.
DR   HOGENOM; HOG000280165; -.
DR   KO; K02393; -.
DR   OMA; STRVANA; -.
DR   Proteomes; UP000002700; Chromosome I.
DR   GO; GO:0009427; C:bacterial-type flagellum basal body, distal rod, L ring; IEA:InterPro.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003774; F:motor activity; IEA:InterPro.
DR   GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:InterPro.
DR   HAMAP; MF_00415; FlgH; 1.
DR   InterPro; IPR000527; Flag_Lring.
DR   PANTHER; PTHR34933; PTHR34933; 1.
DR   Pfam; PF02107; FlgH; 1.
DR   PRINTS; PR01008; FLGLRINGFLGH.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3JX21.
DR   SWISS-2DPAGE; Q3JX21.
KW   Bacterial flagellum; Cell outer membrane; Lipoprotein; Membrane; Palmitate;
KW   Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
FT   CHAIN           19..222
FT                   /note="Flagellar L-ring protein"
FT                   /id="PRO_0000236816"
FT   LIPID           19
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
FT   LIPID           19
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
SQ   SEQUENCE   222 AA;  23349 MW;  3A8A4753F76F705F CRC64;
     MRRPGAAALA AAALALAGCA QIPREPITQQ PMSAMPPMPP AMQAPGSIYN PGYAGRPLFE
     DQRPRNVGDI LTIVIAENIN ATKSSGANTN RQGNTSFDVP TAGFLGGLFN KANLSAQGAN
     KFAATGGASA ANTFNGTITV TVTNVLPNGN LVVSGEKQML INQGNEFVRF SGIVNPNTIS
     GQNSVYSTQV ADARIEYSAK GYINEAETMG WLQRFFLNIA PW
//

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