ID FLAX_SULAC Reviewed; 250 AA. AC Q4J9K6; DT 24-JUL-2024, integrated into UniProtKB/Swiss-Prot. DT 02-AUG-2005, sequence version 1. DT 24-JUL-2024, entry version 72. DE RecName: Full=Archaeal flagellar motor scaffold protein FlaX {ECO:0000305}; GN Name=flaX {ECO:0000303|PubMed:22081969}; GN OrderedLocusNames=Saci_1177 {ECO:0000312|EMBL:AAY80524.1}; OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC OS 15157 / NCIMB 11770). OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Sulfolobus. OX NCBI_TaxID=330779; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770; RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005; RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E., RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.; RT "The genome of Sulfolobus acidocaldarius, a model organism of the RT Crenarchaeota."; RL J. Bacteriol. 187:4992-4999(2005). RN [2] RP FUNCTION, ACTIVITY REGULATION, SUBUNIT, INDUCTION, AND DISRUPTION RP PHENOTYPE. RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770; RX PubMed=22081969; DOI=10.1111/j.1365-2958.2011.07916.x; RA Lassak K., Neiner T., Ghosh A., Klingl A., Wirth R., Albers S.V.; RT "Molecular analysis of the crenarchaeal flagellum."; RL Mol. Microbiol. 83:110-124(2012). RN [3] RP FUNCTION, SUBUNIT, INTERACTION WITH FLAI, SUBCELLULAR LOCATION, AND DOMAIN. RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770; RX PubMed=23129770; DOI=10.1074/jbc.m112.414383; RA Banerjee A., Ghosh A., Mills D.J., Kahnt J., Vonck J., Albers S.V.; RT "FlaX, a unique component of the crenarchaeal archaellum, forms oligomeric RT ring-shaped structures and interacts with the motor ATPase FlaI."; RL J. Biol. Chem. 287:43322-43330(2012). RN [4] RP FUNCTION, SUBUNIT, INTERACTION WITH FLAH AND FLAI, AND SUBCELLULAR RP LOCATION. RX PubMed=24103130; DOI=10.1111/febs.12534; RA Banerjee A., Neiner T., Tripp P., Albers S.V.; RT "Insights into subunit interactions in the Sulfolobus acidocaldarius RT archaellum cytoplasmic complex."; RL FEBS J. 280:6141-6149(2013). RN [5] RP FUNCTION, INTERACTION WITH FLAH, AND DOMAIN. RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770; RX PubMed=26508112; DOI=10.1111/mmi.13260; RA Chaudhury P., Neiner T., D'Imprima E., Banerjee A., Reindl S., Ghosh A., RA Arvai A.S., Mills D.J., van der Does C., Tainer J.A., Vonck J., RA Albers S.V.; RT "The nucleotide-dependent interaction of FlaH and FlaI is essential for RT assembly and function of the archaellum motor."; RL Mol. Microbiol. 99:674-685(2016). RN [6] RP INTERACTION WITH FLAH. RX PubMed=29605923; DOI=10.1007/978-1-4939-7759-8_19; RA Chaudhury P., Tripp P., Albers S.V.; RT "Expression, Purification, and Assembly of Archaellum Subcomplexes of RT Sulfolobus acidocaldarius."; RL Methods Mol. Biol. 1764:307-314(2018). CC -!- FUNCTION: Component of the archaellum (PubMed:22081969, CC PubMed:23129770, PubMed:24103130, PubMed:26508112). FlaX, FlaH and FlaI CC form the core cytoplasmic motor complex of the crenarchaeal archaellum CC (PubMed:24103130, PubMed:26508112). FlaX forms a ring that may act as a CC membrane-bound cytoplasmic scaffold that guides the assembly of the CC archaellum motor complex (PubMed:24103130). Is essential for archaellum CC assembly (PubMed:23129770). {ECO:0000269|PubMed:22081969, CC ECO:0000269|PubMed:23129770, ECO:0000269|PubMed:24103130, CC ECO:0000269|PubMed:26508112}. CC -!- ACTIVITY REGULATION: The presence of the flagellar core components CC FlaH, FlaI and FlaJ seems to be crucial for the stability of FlaX. CC {ECO:0000269|PubMed:22081969}. CC -!- SUBUNIT: The S.acidocaldarius archaellum assembly machinery and its CC filament consist of seven proteins (FlaB, FlaF, FlaG, FlaH, FlaI, FlaJ CC and FlaX) (PubMed:22081969). FlaX assembles into ring-shaped oligomers CC (PubMed:23129770). Interacts directly with FlaH and the motor ATPase CC FlaI (PubMed:23129770, PubMed:24103130, PubMed:26508112, CC PubMed:29605923). {ECO:0000269|PubMed:22081969, CC ECO:0000269|PubMed:23129770, ECO:0000269|PubMed:24103130, CC ECO:0000269|PubMed:26508112, ECO:0000269|PubMed:29605923}. CC -!- INTERACTION: CC Q4J9K6; Q4J9L0: Saci_1173; NbExp=5; IntAct=EBI-8759763, EBI-8759747; CC -!- SUBCELLULAR LOCATION: Archaeal flagellum {ECO:0000269|PubMed:23129770, CC ECO:0000269|PubMed:24103130}. Cell membrane CC {ECO:0000305|PubMed:23129770}; Single-pass membrane protein CC {ECO:0000255}; Cytoplasmic side {ECO:0000305|PubMed:23129770}. CC -!- INDUCTION: Part of the fla operon, which encodes the seven fla genes CC essential for crenarchaeal flagellum assembly and function CC (PubMed:22081969). Expression is induced by tryptone starvation CC (PubMed:22081969). {ECO:0000269|PubMed:22081969}. CC -!- DOMAIN: The C terminal region is involved in the oligomerization, but CC is also essential for interaction with FlaH and FlaI. CC {ECO:0000269|PubMed:23129770, ECO:0000269|PubMed:26508112}. CC -!- DISRUPTION PHENOTYPE: The deletion mutant lacks flagella and is non- CC motile. {ECO:0000269|PubMed:22081969}. 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; CP000077; AAY80524.1; -; Genomic_DNA. DR RefSeq; WP_011278026.1; NZ_CP046615.1. DR AlphaFoldDB; Q4J9K6; -. DR IntAct; Q4J9K6; 1. DR MINT; Q4J9K6; -. DR STRING; 330779.Saci_1177; -. DR GeneID; 78441523; -. DR KEGG; sai:Saci_1177; -. DR PATRIC; fig|330779.12.peg.1141; -. DR eggNOG; arCOG07206; Archaea. DR HOGENOM; CLU_1096748_0_0_2; -. DR Proteomes; UP000001018; Chromosome. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. PE 1: Evidence at protein level; KW Archaeal flagellum; Archaeal flagellum biogenesis; Cell membrane; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1..250 FT /note="Archaeal flagellar motor scaffold protein FlaX" FT /id="PRO_0000460732" FT TOPO_DOM 1..9 FT /note="Extracellular" FT /evidence="ECO:0000305|PubMed:23129770" FT TRANSMEM 10..30 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 31..250 FT /note="Cytoplasmic" FT /evidence="ECO:0000305|PubMed:23129770" SQ SEQUENCE 250 AA; 28056 MW; D5FBFCA640DF8E89 CRC64; MAIQDLLQSS LFIILIGVGI PIAAFLEILF RVILPKTKRV QTQQSPQNIS QEQRFPTQQK PANDETSKYS SDSIEKALKD VLGKMDKKEN ELLTNITNSF NEMKKLIENL NSAVEELALS VKASESDSSS PFNTIIQQEE EHVSREISTV SQLVGSNNPN NVNLTWFIKS CVLLEIMEYD EEKIKQLYEL GYVSSDDMFT ILRILSFIKN RKITAKELAS IAANIAESYS SLTPEIKKYI MILEGGGVNG //