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Database: UniProt
Entry: B2FQC3_STRMK
LinkDB: B2FQC3_STRMK
Original site: B2FQC3_STRMK 
ID   B2FQC3_STRMK            Unreviewed;       702 AA.
AC   B2FQC3;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Flagellar biosynthesis protein FlhA {ECO:0000256|RuleBase:RU364093};
GN   Name=flhA {ECO:0000256|RuleBase:RU364093,
GN   ECO:0000313|EMBL:CAQ45768.1};
GN   OrderedLocusNames=Smlt2273 {ECO:0000313|EMBL:CAQ45768.1};
OS   Stenotrophomonas maltophilia (strain K279a).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=522373 {ECO:0000313|EMBL:CAQ45768.1, ECO:0000313|Proteomes:UP000008840};
RN   [1] {ECO:0000313|EMBL:CAQ45768.1, ECO:0000313|Proteomes:UP000008840}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K279a {ECO:0000313|EMBL:CAQ45768.1,
RC   ECO:0000313|Proteomes:UP000008840};
RX   PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA   Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA   Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA   Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA   Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA   Parkhill J., Thomson N.R., Avison M.B.;
RT   "The complete genome, comparative and functional analysis of
RT   Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT   resistance determinants.";
RL   Genome Biol. 9:R74.1-R74.13(2008).
CC   -!- FUNCTION: Required for formation of the rod structure of the flagellar
CC       apparatus. Together with FliI and FliH, may constitute the export
CC       apparatus of flagellin. {ECO:0000256|RuleBase:RU364093}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU364093};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU364093}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the FHIPEP (flagella/HR/invasion proteins export
CC       pore) family. {ECO:0000256|ARBA:ARBA00008835,
CC       ECO:0000256|RuleBase:RU364093}.
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DR   EMBL; AM743169; CAQ45768.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2FQC3; -.
DR   EnsemblBacteria; CAQ45768; CAQ45768; Smlt2273.
DR   KEGG; sml:Smlt2273; -.
DR   PATRIC; fig|522373.3.peg.2168; -.
DR   eggNOG; COG1298; Bacteria.
DR   HOGENOM; CLU_015346_3_0_6; -.
DR   Proteomes; UP000008840; Chromosome.
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   Gene3D; 3.40.30.60; FHIPEP family, domain 1; 1.
DR   Gene3D; 1.10.8.540; FHIPEP family, domain 3; 1.
DR   Gene3D; 3.40.50.12790; FHIPEP family, domain 4; 1.
DR   InterPro; IPR042194; FHIPEP_1.
DR   InterPro; IPR042193; FHIPEP_3.
DR   InterPro; IPR042196; FHIPEP_4.
DR   InterPro; IPR006301; FlhA.
DR   InterPro; IPR001712; T3SS_FHIPEP.
DR   NCBIfam; TIGR01398; FlhA; 1.
DR   PANTHER; PTHR30161:SF1; FLAGELLAR BIOSYNTHESIS PROTEIN FLHA-RELATED; 1.
DR   PANTHER; PTHR30161; FLAGELLAR EXPORT PROTEIN, MEMBRANE FLHA SUBUNIT-RELATED; 1.
DR   Pfam; PF00771; FHIPEP; 1.
DR   PIRSF; PIRSF005419; FlhA; 1.
DR   PRINTS; PR00949; TYPE3IMAPROT.
PE   3: Inferred from homology;
KW   Bacterial flagellum biogenesis {ECO:0000256|RuleBase:RU364093};
KW   Bacterial flagellum protein export {ECO:0000256|RuleBase:RU364093};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|RuleBase:RU364093};
KW   Cell projection {ECO:0000313|EMBL:CAQ45768.1};
KW   Cilium {ECO:0000313|EMBL:CAQ45768.1};
KW   Flagellum {ECO:0000313|EMBL:CAQ45768.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364093};
KW   Protein transport {ECO:0000256|RuleBase:RU364093};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008840};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU364093};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU364093}; Transport {ECO:0000256|RuleBase:RU364093}.
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364093"
FT   TRANSMEM        47..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364093"
FT   TRANSMEM        72..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364093"
FT   TRANSMEM        117..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364093"
FT   TRANSMEM        209..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364093"
FT   TRANSMEM        251..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364093"
FT   TRANSMEM        289..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364093"
SQ   SEQUENCE   702 AA;  74373 MW;  B875DBF7FF72EA32 CRC64;
     MSAQPSAGFN TRRALEMIRQ GLGAPLIVLA LLAMVVVPLA APVLDALFTF NIAISLMVLL
     AVVYVKRPLD FTIFPIVLLI TTMLRLALNV ASTRVILLNG QNGHDAAGKV IAAFGEFVIG
     GNYAVGIVVF AILTIINFVV ITKGAGRVSE VTARFILDAM PGKQMAIDAD LNAGLLTREE
     AKLRREEVRE EADFYGAMDG ASKFIRGDAI AGILILFINM LGGLAVGVLQ HGMPFGEAAA
     TYTLLSIGDG LVAQLPALLV SSAVAMLVTR ASRSQDMAQA MTGQVFGQYR ALAITAGIIG
     VVGLVPGMPN VAFLTLAAIL GFIAWKVYRK GKAAATDPAA AGNDAAALNA LGRPAAPAPT
     AELSWDELRP VDPLGLEVGY RLIPLVDSNQ GGELMARIKG VRRKLTQDVG FLIPSVHIRD
     NLELPANGYR VLVHGVPVAT AEIHPDRELA LDPGSALGTL EGIAGKDPAF GLDATWIQPH
     QRAQAETLGY TVVDPATVVA THLSHLIREH APELLGHEEV QHLLANLAKS APKLVEDLTP
     KALPLSAVVR VLQNLLVERI PIRQLRKIAE ALVEHAPSSQ DPAVLTAAVR TALGRFIVQE
     IAGMSAELPV FTLNPQLERV LQESTQGNGA ALEPGLAERL HQSLAECVSK QEARNEPAVV
     LVPGPVRAAL ARLVRHSVPS LSVLAYSEVP EDKRLKLVGT IS
//
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