ID A0A2S5SYJ0_9BURK Unreviewed; 377 AA.
AC A0A2S5SYJ0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, 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 ORFNames=C1704_02965 {ECO:0000313|EMBL:PPE67835.1};
OS Caldimonas caldifontis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Caldimonas.
OX NCBI_TaxID=1452508 {ECO:0000313|EMBL:PPE67835.1, ECO:0000313|Proteomes:UP000238605};
RN [1] {ECO:0000313|EMBL:PPE67835.1, ECO:0000313|Proteomes:UP000238605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCRC 80649 {ECO:0000313|EMBL:PPE67835.1,
RC ECO:0000313|Proteomes:UP000238605};
RA Tang B.;
RT "Reclassifiation of [Polyangium] brachysporum DSM 7029 as Guopingzhaonella
RT breviflexa gen. nov., sp. nov., a member of the family Comamonadaceae.";
RL Submitted (FEB-2018) 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}.
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:PPE67835.1}.
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DR EMBL; PSNX01000002; PPE67835.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S5SYJ0; -.
DR OrthoDB; 9786431at2; -.
DR Proteomes; UP000238605; 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:PPE67835.1};
KW Cilium {ECO:0000313|EMBL:PPE67835.1};
KW Flagellum {ECO:0000313|EMBL:PPE67835.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000238605};
KW Signal {ECO:0000256|HAMAP-Rule:MF_00416}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT CHAIN 33..377
FT /note="Flagellar P-ring protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT /id="PRO_5015792608"
SQ SEQUENCE 377 AA; 38655 MW; E6A6A1947EB08020 CRC64;
MNTPSDRFLR MAIALAALAA STALWWPLPA QAQRIKEVAS VQGVRPNQLI GYGLVVGLDG
TGDQTTQTPF TAQSIAAMLQ QMGVTVPPGV NMQLKNVAAV MVTAQLPAFA QPGQAIDVNV
ASLGNAKSLR GGMLIATPLK GADGNIYALA QGNLIVGGAG ASAGGSKVQV NHLSAGRIPA
GATVERSVPT PLHQGEFLQL DLNAADFHTA RQVAQAINRA KGEGVAEAMD GRTVRVRAPQ
SPGERVAFLA DIENLPVQGA APAAKVVLNA RTGSIVMNQA VTLLPAAVAH GNLSVTISST
PVISQPAPFS RGETVVAEQA DIQIRQDGGS LIEVPAGTKL TDVVRALNSL GATPMDLLAI
LQAMKAAGAL QAELEVI
//
