ID F5Z573_ALTNA Unreviewed; 293 AA.
AC F5Z573;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Flagellar L-ring protein {ECO:0000313|EMBL:AEF04719.1};
GN OrderedLocusNames=ambt_16060 {ECO:0000313|EMBL:AEF04719.1};
OS Alteromonas naphthalenivorans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX NCBI_TaxID=715451 {ECO:0000313|EMBL:AEF04719.1, ECO:0000313|Proteomes:UP000000683};
RN [1] {ECO:0000313|EMBL:AEF04719.1, ECO:0000313|Proteomes:UP000000683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 17741 / KACC 18427 / KCTC 11700BP / SN2
RC {ECO:0000313|Proteomes:UP000000683};
RX PubMed=21705606; DOI=10.1128/JB.05252-11;
RA Jin H.M., Jeong H., Moon E.J., Math R.K., Lee K., Kim H.J., Jeon C.O.,
RA Oh T.K., Kim J.F.;
RT "Complete genome sequence of the polycyclic aromatic hydrocarbon-degrading
RT bacterium Alteromonas sp. strain SN2.";
RL J. Bacteriol. 193:4292-4293(2011).
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}.
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}.
CC -!- SUBCELLULAR LOCATION: Bacterial flagellum basal body
CC {ECO:0000256|ARBA:ARBA00004117}. Membrane
CC {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004635}.
CC -!- SIMILARITY: Belongs to the FlgH family.
CC {ECO:0000256|ARBA:ARBA00006929}.
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DR EMBL; CP002339; AEF04719.1; -; Genomic_DNA.
DR AlphaFoldDB; F5Z573; -.
DR KEGG; alt:ambt_16060; -.
DR eggNOG; COG2063; Bacteria.
DR HOGENOM; CLU_069313_0_2_6; -.
DR Proteomes; UP000000683; Chromosome.
DR GO; GO:0009427; C:bacterial-type flagellum basal body, distal rod, L ring; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:InterPro.
DR InterPro; IPR000527; Flag_Lring.
DR PANTHER; PTHR34933; FLAGELLAR L-RING PROTEIN; 1.
DR PANTHER; PTHR34933:SF1; FLAGELLAR L-RING PROTEIN; 1.
DR Pfam; PF02107; FlgH; 1.
DR PRINTS; PR01008; FLGLRINGFLGH.
PE 3: Inferred from homology;
KW Bacterial flagellum {ECO:0000256|ARBA:ARBA00023143};
KW Cell projection {ECO:0000313|EMBL:AEF04719.1};
KW Cilium {ECO:0000313|EMBL:AEF04719.1};
KW Flagellum {ECO:0000313|EMBL:AEF04719.1};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT REGION 74..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 293 AA; 32696 MW; 2A23FA6257E9C838 CRC64;
MFCKGFAKLL KNVFRVEIIR LNLLLFGSWM ALNQRYFLFP SEHIMKIRCQ KVFLALIFTM
TGCAQTVSHE EEVVASSPTN PKVEQRAISP TSDEPAPGDP TYAPPRAYSV EQVRIPSGSL
FNPELAMGLY QRHSQYKVGD MILIKLDETT QSEKSLDYNQ DKNSTFDIEP LTVRVGGIQI
EGDDLEVDHE QDSEFTSSAQ SSQSNSLQGS ITVYVTAITP AGNLLVTGEK WITMNKGKEY
IRFSGEVRKQ DVDESNTVVS SKVGNALIEY SGTGDLQENQ ERSVIDKLFA IFG
//
