ID A0A1H9BZG5_9RHOB Unreviewed; 368 AA.
AC A0A1H9BZG5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Flagellar P-ring protein {ECO:0000256|ARBA:ARBA00019515, ECO:0000256|HAMAP-Rule:MF_00416};
DE AltName: Full=Basal body P-ring protein {ECO:0000256|ARBA:ARBA00032344, ECO:0000256|HAMAP-Rule:MF_00416};
DE Flags: Precursor;
GN Name=flgI {ECO:0000256|HAMAP-Rule:MF_00416};
GN ORFNames=SAMN04488092_10359 {ECO:0000313|EMBL:SEP94157.1};
OS Thalassovita taeanensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Thalassovita.
OX NCBI_TaxID=657014 {ECO:0000313|EMBL:SEP94157.1, ECO:0000313|Proteomes:UP000198634};
RN [1] {ECO:0000313|EMBL:SEP94157.1, ECO:0000313|Proteomes:UP000198634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22007 {ECO:0000313|EMBL:SEP94157.1,
RC ECO:0000313|Proteomes:UP000198634};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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|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}.
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DR EMBL; FOEP01000003; SEP94157.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9BZG5; -.
DR STRING; 657014.SAMN04488092_10359; -.
DR OrthoDB; 9786431at2; -.
DR Proteomes; UP000198634; 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:SEP94157.1};
KW Cilium {ECO:0000313|EMBL:SEP94157.1};
KW Flagellum {ECO:0000313|EMBL:SEP94157.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198634};
KW Signal {ECO:0000256|HAMAP-Rule:MF_00416}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT CHAIN 22..368
FT /note="Flagellar P-ring protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT /id="PRO_5009356508"
SQ SEQUENCE 368 AA; 38458 MW; 0506403584FBA276 CRC64;
MKQFLLSLFV TAVLLASEAH AGAIRIKDLV EFDGVRGNDL VGYGLVVGLN GTGDGIRNAP
FTEEIMSNIL ERLGVNVTGE QFRPKNVAAV FVTASLPPFA RAGGRIDVTV SAIGDAKSLL
GGTLIMTPLN AADGQIYAVA QGTIIAGGAS AEGEAASVVQ GVPTSGVVPS GAHVEREVDF
DFSSLSSLRI ALREPDFTTA GRIERAINSD FGSRVAVMLD SGTIQLDIPA TRMRSPAHAL
GRIENISVQP ERKARVVVDQ RSGTIVMGED VRISRVAVSQ GNLTLRIQEA PLAVQPNPFS
EGETVVVPRS RADITEEEGT GLAEVSGGTS LSEVVAGLNA LGVSPRDMID ILKSIKAAGA
LHAEFLVR
//
