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FLGH_PHOPR
ID   FLGH_PHOPR              Reviewed;         256 AA.
AC   Q6LTQ7;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Flagellar L-ring protein;
DE   AltName: Full=Basal body L-ring protein;
DE   Flags: Precursor;
GN   Name=flgH; OrderedLocusNames=PBPRA0907;
OS   Photobacterium profundum (strain SS9).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=298386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1253 / SS9;
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA   Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA   Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and expression
RT   analysis.";
RL   Science 307:1459-1461(2005).
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:0000250}.
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Lipid-anchor
CC       {ECO:0000250}. Bacterial flagellum basal body {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FlgH family. {ECO:0000305}.
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DR   EMBL; CR378665; CAG19318.1; -; Genomic_DNA.
DR   RefSeq; WP_011217655.1; NC_006370.1.
DR   AlphaFoldDB; Q6LTQ7; -.
DR   SMR; Q6LTQ7; -.
DR   STRING; 298386.PBPRA0907; -.
DR   EnsemblBacteria; CAG19318; CAG19318; PBPRA0907.
DR   KEGG; ppr:PBPRA0907; -.
DR   eggNOG; COG2063; Bacteria.
DR   HOGENOM; CLU_069313_0_2_6; -.
DR   OMA; ITQQPMT; -.
DR   OrthoDB; 1900876at2; -.
DR   Proteomes; UP000000593; Chromosome 1.
DR   GO; GO:0009427; C:bacterial-type flagellum basal body, distal rod, L ring; IEA:InterPro.
DR   GO; GO:0009279; C:cell outer 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   HAMAP; MF_00415; FlgH; 1.
DR   InterPro; IPR000527; Flag_Lring.
DR   PANTHER; PTHR34933; PTHR34933; 1.
DR   Pfam; PF02107; FlgH; 1.
DR   PRINTS; PR01008; FLGLRINGFLGH.
PE   3: Inferred from homology;
KW   Bacterial flagellum; Cell outer membrane; Lipoprotein; Membrane; Palmitate;
KW   Reference proteome; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..256
FT                   /note="Flagellar L-ring protein"
FT                   /id="PRO_0000009458"
FT   LIPID           16
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   LIPID           16
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   256 AA;  27752 MW;  BBE9192F6D2976EE CRC64;
     MKKVLAGIVI LLLNGCAMDP DLAPSDIEKA TTTVDAVEGS TEQDSGLIDM LRRREDPQAG
     DPAWNPIRPQ AKPEHYATAT GSLFSSIQAQ DLYDDTKPRG IGDIVTVMLE EKTQAKKSAS
     SDLDKSTDLS MDPLVLGGKP LTIGDRDLSY EVANANKFSG TTSADQSNSI KGSISVEVID
     VLANGNLMIR GEKWLTLNTG DEYIRVSGTI RPDDISQENT IESTRITNAR IQYSGTGNRQ
     DVQEQGWLAN FFNVSL
 
 
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