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Database: UniProt
Entry: A0A1Y0G7Z7_9PROT
LinkDB: A0A1Y0G7Z7_9PROT
Original site: A0A1Y0G7Z7_9PROT 
ID   A0A1Y0G7Z7_9PROT        Unreviewed;        89 AA.
AC   A0A1Y0G7Z7;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Flagellar biosynthetic protein FliQ {ECO:0000256|ARBA:ARBA00021718, ECO:0000256|RuleBase:RU364090};
GN   Name=fliQ {ECO:0000256|RuleBase:RU364090};
GN   ORFNames=CAP31_08260 {ECO:0000313|EMBL:ARU31676.1};
OS   Sulfuriferula sp. AH1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Sulfuricellaceae; Sulfuriferula.
OX   NCBI_TaxID=1985873 {ECO:0000313|EMBL:ARU31676.1, ECO:0000313|Proteomes:UP000195558};
RN   [1] {ECO:0000313|EMBL:ARU31676.1, ECO:0000313|Proteomes:UP000195558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AH1 {ECO:0000313|EMBL:ARU31676.1,
RC   ECO:0000313|Proteomes:UP000195558};
RA   Jones D.S., Hua A.A., Roepke E.W., Bailey J.V.;
RT   "The complete genome sequence of Sulfuriferula sp. str. AH1, a sulfur-
RT   oxidizing autotroph isolated from weathered sulfide-bearing rock from the
RT   Duluth Complex.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Role in flagellar biosynthesis.
CC       {ECO:0000256|RuleBase:RU364090}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU364090}.
CC       Bacterial flagellum basal body {ECO:0000256|RuleBase:RU364090}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the FliQ/MopD/SpaQ family.
CC       {ECO:0000256|ARBA:ARBA00006156, ECO:0000256|RuleBase:RU364090}.
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DR   EMBL; CP021138; ARU31676.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y0G7Z7; -.
DR   KEGG; sulf:CAP31_08260; -.
DR   OrthoDB; 9806440at2; -.
DR   Proteomes; UP000195558; Chromosome.
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:0044780; P:bacterial-type flagellum assembly; IEA:InterPro.
DR   GO; GO:0009306; P:protein secretion; IEA:InterPro.
DR   InterPro; IPR002191; Bac_export_3.
DR   InterPro; IPR006305; FliQ.
DR   InterPro; IPR006306; T3SS_HrpO.
DR   NCBIfam; TIGR01402; fliQ; 1.
DR   NCBIfam; TIGR01403; fliQ_rel_III; 1.
DR   PANTHER; PTHR34040; FLAGELLAR BIOSYNTHETIC PROTEIN FLIQ; 1.
DR   PANTHER; PTHR34040:SF2; FLAGELLAR BIOSYNTHETIC PROTEIN FLIQ; 1.
DR   Pfam; PF01313; Bac_export_3; 1.
DR   PIRSF; PIRSF004669; FliQ; 1.
DR   PRINTS; PR00952; TYPE3IMQPROT.
PE   3: Inferred from homology;
KW   Bacterial flagellum {ECO:0000256|ARBA:ARBA00023143,
KW   ECO:0000256|RuleBase:RU364090};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|RuleBase:RU364090};
KW   Cell projection {ECO:0000313|EMBL:ARU31676.1};
KW   Cilium {ECO:0000313|EMBL:ARU31676.1};
KW   Flagellum {ECO:0000313|EMBL:ARU31676.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364090};
KW   Reference proteome {ECO:0000313|Proteomes:UP000195558};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU364090};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU364090}.
FT   TRANSMEM        20..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364090"
FT   TRANSMEM        51..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364090"
SQ   SEQUENCE   89 AA;  9686 MW;  C07D7AA6D5762D96 CRC64;
     MTPESVMTIG RHALEVTLMV SAPMLLVALI IGLIVSIFQA ATQINETTLS FIPKLVGIFI
     TLVVAGPWML SVLLDYMREV FTNIPNLVG
//
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