ID A0A4U8SEI8_9HELI Unreviewed; 367 AA.
AC A0A4U8SEI8;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 13-SEP-2023, entry version 11.
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 {ECO:0000256|HAMAP-Rule:MF_00416,
GN ECO:0000313|EMBL:TLD84563.1};
GN ORFNames=LS70_003170 {ECO:0000313|EMBL:TLD84563.1};
OS Helicobacter sp. MIT 11-5569.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1548151 {ECO:0000313|EMBL:TLD84563.1, ECO:0000313|Proteomes:UP000029923};
RN [1] {ECO:0000313|EMBL:TLD84563.1, ECO:0000313|Proteomes:UP000029923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 11-5569 {ECO:0000313|EMBL:TLD84563.1,
RC ECO:0000313|Proteomes:UP000029923};
RX PubMed=25428971;
RA Sheh A., Shen Z., Fox J.G.;
RT "Draft genome sequences of eight enterohepatic helicobacter species
RT isolated from both laboratory and wild rodents.";
RL Genome Announc. 2:e01218-e01214(2014).
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|HAMAP-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|HAMAP-
CC Rule:MF_00416}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TLD84563.1}.
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DR EMBL; JRPB02000002; TLD84563.1; -; Genomic_DNA.
DR RefSeq; WP_034289929.1; NZ_JRPB02000002.1.
DR AlphaFoldDB; A0A4U8SEI8; -.
DR STRING; 1548151.LS70_06130; -.
DR OrthoDB; 9786431at2; -.
DR Proteomes; UP000029923; 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:TLD84563.1};
KW Cilium {ECO:0000313|EMBL:TLD84563.1};
KW Flagellum {ECO:0000313|EMBL:TLD84563.1};
KW Signal {ECO:0000256|HAMAP-Rule:MF_00416}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT CHAIN 23..367
FT /note="Flagellar P-ring protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT /id="PRO_5021058588"
FT REGION 206..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 367 AA; 38918 MW; 670D0F93AA652CEB CRC64;
MKTTKFFKLL VLCLIFALPA FSAKISDLAN IVGVRDNQLI GYGLVVGLNG TGDKTTSTFT
MQSISNMLDS VNVKIDANDI SSKNVAAVMV TAKLPAFARQ GDKIDILVSS IGDAKSLEGG
TLLLTPLSGL DGRIYAVAQG AVGIGGKSER GGSANHPLAG LLPNGATVER EVSYDLYNKI
NATLSLKESN FQNAMRIQRS INAAFAQEQQ AQPQEGQATQ TPPTPVATAI DPRTIKLQRP
QEMSMVEFLA RVQEIDIDAI KEDKIIINER TGTIIAGMGV EVSPIVVTHN NITIKVSNEA
TTDPEAVNMG NGATFSAAEA TLSAQNNPTI SSVTRALQRM GATPKDMIAI LETMKKAGAF
NADLEII
//