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Database: UniProt
Entry: F4MZV1_YEREN
LinkDB: F4MZV1_YEREN
Original site: F4MZV1_YEREN 
ID   F4MZV1_YEREN            Unreviewed;       138 AA.
AC   F4MZV1;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Flagellar motor switch protein FliN {ECO:0000256|ARBA:ARBA00021897, ECO:0000256|RuleBase:RU362074};
GN   Name=fliN {ECO:0000313|EMBL:CBX71359.1};
GN   ORFNames=YEW_KR45510 {ECO:0000313|EMBL:CBX71359.1};
OS   Yersinia enterocolitica W22703.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=913028 {ECO:0000313|EMBL:CBX71359.1};
RN   [1] {ECO:0000313|EMBL:CBX71359.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21453472; DOI=10.1186/1471-2164-12-168;
RA   Fuchs T.M., Brandt K., Starke M., Rattei T.;
RT   "Shotgun sequencing of Yersinia enterocolitica strain W22703 (biotype 2,
RT   serotype O:9): genomic evidence for oscillation between invertebrates and
RT   mammals.";
RL   BMC Genomics 12:168-168(2011).
CC   -!- FUNCTION: FliN is one of three proteins (FliG, FliN, FliM) that form
CC       the rotor-mounted switch complex (C ring), located at the base of the
CC       basal body. This complex interacts with the CheY and CheZ chemotaxis
CC       proteins, in addition to contacting components of the motor that
CC       determine the direction of flagellar rotation.
CC       {ECO:0000256|RuleBase:RU362074}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362074};
CC       Peripheral membrane protein {ECO:0000256|RuleBase:RU362074};
CC       Cytoplasmic side {ECO:0000256|RuleBase:RU362074}. Bacterial flagellum
CC       basal body {ECO:0000256|RuleBase:RU362074}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004287}.
CC   -!- SIMILARITY: Belongs to the FliN/MopA/SpaO family.
CC       {ECO:0000256|ARBA:ARBA00009226, ECO:0000256|RuleBase:RU362074}.
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DR   EMBL; FR718584; CBX71359.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4MZV1; -.
DR   GO; GO:0009425; C:bacterial-type flagellum basal body; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:UniProtKB-UniRule.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.330.10; SpoA-like; 1.
DR   InterPro; IPR012826; FliN.
DR   InterPro; IPR001543; FliN-like_C.
DR   InterPro; IPR031576; FliN_N.
DR   InterPro; IPR001172; FliN_T3SS_HrcQb.
DR   InterPro; IPR036429; SpoA-like_sf.
DR   NCBIfam; TIGR02480; fliN; 1.
DR   PANTHER; PTHR43484; -; 1.
DR   PANTHER; PTHR43484:SF1; FLAGELLAR MOTOR SWITCH PROTEIN FLIN; 1.
DR   Pfam; PF01052; FliMN_C; 1.
DR   Pfam; PF16973; FliN_N; 1.
DR   PRINTS; PR00956; FLGMOTORFLIN.
DR   SUPFAM; SSF101801; Surface presentation of antigens (SPOA); 1.
PE   3: Inferred from homology;
KW   Bacterial flagellum {ECO:0000256|RuleBase:RU362074};
KW   Cell membrane {ECO:0000256|RuleBase:RU362074};
KW   Cell projection {ECO:0000313|EMBL:CBX71359.1};
KW   Chemotaxis {ECO:0000256|ARBA:ARBA00022500, ECO:0000256|RuleBase:RU362074};
KW   Cilium {ECO:0000313|EMBL:CBX71359.1};
KW   Flagellar rotation {ECO:0000256|RuleBase:RU362074};
KW   Flagellum {ECO:0000313|EMBL:CBX71359.1};
KW   Membrane {ECO:0000256|RuleBase:RU362074}.
FT   DOMAIN          1..50
FT                   /note="Flagellar motor switch protein FliN N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16973"
FT   DOMAIN          57..127
FT                   /note="Flagellar motor switch protein FliN-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01052"
SQ   SEQUENCE   138 AA;  14978 MW;  27CD6B8DE55A297D CRC64;
     MSDPKLPSDD GKESVDDLWA DAFNEQLASD KPAATTDGVF KSLEAPDALG NLQDIDLILD
     IPVKLTVELG RTKMTIKELL RLSQGSVVSL DGLAGEPLDI LINGYLIAQG EVVVVADKYG
     VRITDIITPS ERMRRLSR
//
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