ID K5XSR0_9PROT Unreviewed; 366 AA.
AC K5XSR0;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
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=MXAZACID_09396 {ECO:0000313|EMBL:EKM99644.1};
OS Acidocella sp. MX-AZ02.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidocella.
OX NCBI_TaxID=1214225 {ECO:0000313|EMBL:EKM99644.1, ECO:0000313|Proteomes:UP000006217};
RN [1] {ECO:0000313|EMBL:EKM99644.1, ECO:0000313|Proteomes:UP000006217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MX-AZ02 {ECO:0000313|EMBL:EKM99644.1,
RC ECO:0000313|Proteomes:UP000006217};
RX PubMed=23405365;
RA Servin-Garciduenas L.E., Garrett R.A., Amils R., Martinez-Romero E.;
RT "Genome Sequence of the Acidophilic Bacterium Acidocella sp. Strain MX-
RT AZ02.";
RL Genome Announc. 1:E00041-12(2013).
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:EKM99644.1}.
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DR EMBL; AMPS01000137; EKM99644.1; -; Genomic_DNA.
DR RefSeq; WP_008494052.1; NZ_JH976208.1.
DR AlphaFoldDB; K5XSR0; -.
DR STRING; 1214225.MXAZACID_09396; -.
DR PATRIC; fig|1214225.3.peg.1827; -.
DR HOGENOM; CLU_045235_1_0_5; -.
DR Proteomes; UP000006217; 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:EKM99644.1};
KW Cilium {ECO:0000313|EMBL:EKM99644.1};
KW Flagellum {ECO:0000313|EMBL:EKM99644.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006217};
KW Signal {ECO:0000256|HAMAP-Rule:MF_00416}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT CHAIN 21..366
FT /note="Flagellar P-ring protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT /id="PRO_5009016144"
SQ SEQUENCE 366 AA; 36481 MW; D4864F0FCE598782 CRC64;
MRICAATLLA LLVFGGKAFA AGDATTIGQL VSVAGAPSNQ LYGYGLVVGL PGTGDQTTQV
PYTQQSILNM LRNMGIALPN VSTMQPNDVA SVMVTAEVPA FAHSGQHADV TVSAVGNATS
LAGGVLLPTP LRGGNGVVYA QAQGPLLVSG FAASAGGTSA SVNVPTVGTL PGGAILATTI
PATYAINGAS ALLLNQPSYQ TAQQIADVIN RYDAGTATAV SPGEVDLSAQ GQDAMRFMAN
VLALPITPVG QAPTIVVDAQ SGTIVMNAGV TLGPAVVSHG DLTVTIQTQN SVSQPGPFSN
GSTVGVRNTA VNAKQSKAQV INLPRAATLQ DVAAALNAVG ATPQDLIAII QALKQAGAIN
GTIKVI
//
