ID A6LMY4_THEM4 Unreviewed; 680 AA.
AC A6LMY4;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Flagellar biosynthesis protein FlhA {ECO:0000256|RuleBase:RU364093};
GN Name=flhA {ECO:0000256|RuleBase:RU364093};
GN OrderedLocusNames=Tmel_1438 {ECO:0000313|EMBL:ABR31285.1};
OS Thermosipho melanesiensis (strain DSM 12029 / CIP 104789 / BI429).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC Thermosipho.
OX NCBI_TaxID=391009 {ECO:0000313|EMBL:ABR31285.1, ECO:0000313|Proteomes:UP000001110};
RN [1] {ECO:0000313|EMBL:ABR31285.1, ECO:0000313|Proteomes:UP000001110}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12029 / CIP 104789 / BI429
RC {ECO:0000313|Proteomes:UP000001110};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT "Complete sequence of Thermosipho melanesiensis BI429.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABR31285.1, ECO:0000313|Proteomes:UP000001110}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12029 / CIP 104789 / BI429
RC {ECO:0000313|Proteomes:UP000001110};
RX PubMed=19307556; DOI=10.1073/pnas.0901260106;
RA Zhaxybayeva O., Swithers K.S., Lapierre P., Fournier G.P., Bickhart D.M.,
RA DeBoy R.T., Nelson K.E., Nesbo C.L., Doolittle W.F., Gogarten J.P.,
RA Noll K.M.;
RT "On the chimeric nature, thermophilic origin, and phylogenetic placement of
RT the Thermotogales.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5865-5870(2009).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000716; ABR31285.1; -; Genomic_DNA.
DR RefSeq; WP_012057644.1; NC_009616.1.
DR AlphaFoldDB; A6LMY4; -.
DR STRING; 391009.Tmel_1438; -.
DR KEGG; tme:Tmel_1438; -.
DR eggNOG; COG1298; Bacteria.
DR HOGENOM; CLU_015346_3_0_0; -.
DR OrthoDB; 9759185at2; -.
DR Proteomes; UP000001110; 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:ABR31285.1};
KW Cilium {ECO:0000313|EMBL:ABR31285.1};
KW Flagellum {ECO:0000313|EMBL:ABR31285.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364093};
KW Protein transport {ECO:0000256|RuleBase:RU364093};
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 7..25
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364093"
FT TRANSMEM 31..50
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364093"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364093"
FT TRANSMEM 102..123
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364093"
FT TRANSMEM 191..213
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364093"
FT TRANSMEM 233..252
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364093"
FT TRANSMEM 273..303
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364093"
SQ SEQUENCE 680 AA; 75132 MW; 05F3A3F953CF18E1 CRC64;
MSKGTDVIVA IMVAAIVLLM ILPIPGFLLD FFQLLNISLS LVILFSTMYI RKALELSSFP
TILLVVTLFR LGLNVASTRL ILLQGPKFSG KVIRAFGDFV VGGNYVVGLV VFLILVIIQF
IVITRGSERI AEVAARFTLD AMPGKQMSVD ADLNAGLITE DEARRRRDEI RREADFYGAM
DGASKFVRGD AIASIIIVLV NIIGGLIIGI LTHKMTVTEA AQTFTLFTVG DGLVTQIPAL
MVSTATGILV SRAASEDNLG TELVKELGSE KKVIILTGGI LIFLGLFTPI PFTAVLIGLL
FLITGSLIKS VSEPEMETAS ISEISERPMG PVLSTPQEVS EIIQTDTVEI EIGYGLIPLA
DTSQGGDLLE RVTMVRKQIA YELGLVISPI RVRDSVLLKS NEYAIFIRGA EVAKYELLPN
RLLAINPGTV LEKIPGIETK EPAFGLQAFW IDESRKEEAT RLGYTVVDPP TVFATHLTEI
LKRHAHELLG SKEFDLLVEG LRDRFDKLVD NLFNVLKPTE VKKVLQKLLK EGISIRNLPL
IFETLLEYGE YTKDIVYLTE KVRKALKRQI ITPLISNDNI LHAIAFDNNL EKSLVNLVKD
LDGEKYLDLN PEIMRELIEN ISKNLENLMK KGYNPVLICS SSLRPLIADL IIKFIPGIYV
VSYDEIPENI TMQIEGVIKL
//
