ID A0A0H5LQW5_YERIN Unreviewed; 369 AA.
AC A0A0H5LQW5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Flagellar P-ring protein {ECO:0000256|HAMAP-Rule:MF_00416};
DE AltName: Full=Basal body P-ring protein {ECO:0000256|HAMAP-Rule:MF_00416};
DE Flags: Precursor;
GN Name=flgI_1 {ECO:0000313|EMBL:CRY53460.1};
GN Synonyms=flgI {ECO:0000256|HAMAP-Rule:MF_00416};
GN ORFNames=ERS008476_00352 {ECO:0000313|EMBL:CRY53460.1};
OS Yersinia intermedia.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=631 {ECO:0000313|EMBL:CRY53460.1, ECO:0000313|Proteomes:UP000043316};
RN [1] {ECO:0000313|Proteomes:UP000043316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R148 {ECO:0000313|Proteomes:UP000043316};
RG Pathogen Informatics;
RL Submitted (MAR-2015) 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:0000256|ARBA:ARBA00002591, ECO:0000256|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:0000256|ARBA:ARBA00011439, ECO:0000256|HAMAP-
CC Rule:MF_00416}.
CC -!- SUBCELLULAR LOCATION: Bacterial flagellum basal body
CC {ECO:0000256|ARBA:ARBA00004117, ECO:0000256|HAMAP-Rule:MF_00416}.
CC -!- SIMILARITY: Belongs to the FlgI family. {ECO:0000256|ARBA:ARBA00008994,
CC ECO:0000256|HAMAP-Rule:MF_00416}.
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DR EMBL; CWJI01000001; CRY53460.1; -; Genomic_DNA.
DR RefSeq; WP_049605639.1; NZ_CWJI01000001.1.
DR AlphaFoldDB; A0A0H5LQW5; -.
DR Proteomes; UP000043316; Unassembled WGS sequence.
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; FLAGELLAR P-RING PERIPLASMIC PROTEIN FLGI; 1.
DR PANTHER; PTHR30381:SF0; FLAGELLAR P-RING PROTEIN; 1.
DR Pfam; PF02119; FlgI; 1.
DR PRINTS; PR01010; FLGPRINGFLGI.
PE 3: Inferred from homology;
KW Bacterial flagellum {ECO:0000256|ARBA:ARBA00023143, ECO:0000256|HAMAP-
KW Rule:MF_00416}; Cell projection {ECO:0000313|EMBL:CRY53460.1};
KW Cilium {ECO:0000313|EMBL:CRY53460.1};
KW Flagellum {ECO:0000313|EMBL:CRY53460.1};
KW Signal {ECO:0000256|HAMAP-Rule:MF_00416}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT CHAIN 24..369
FT /note="Flagellar P-ring protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT /id="PRO_5008989247"
SQ SEQUENCE 369 AA; 38606 MW; 922E6FA11DDDC6CC CRC64;
MRKPSLVTLF ITLLSLVWMP AQAERIRDLV TVQGVRDNAL IGYGLVVGLD GSGDQTMQTP
FTTQSLSNML SQLGITVPPG TNMQLKNVAA VMVTAKLPAF SRAGQTIDVV VSSMGNAKSI
RGGTLLMTPL KGVDNQVYAL AQGNVLVGGA GASSGGSSVQ VNQLTGGRIS NGATIERELP
TTFGTDGVIN LQLNTEDFTM AQQVSDAINR QRGFGSATAI DARTIQVLVP RGNSSQVRFL
ADIQNIPVNV DAGDAKVIIN SRTGSVVMNR NVVLDSCAVA QGNLSVVVDK QNIVSQPDTP
FGGGQTVVTP NTQISVQQQG GVLQRVNASP NLNNVVRALN SLGATPIDLM SILQAMQSAG
CLRAKLEII
//
