SECF_METJA
ID SECF_METJA Reviewed; 282 AA.
AC Q58650;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Protein-export membrane protein SecF {ECO:0000255|HAMAP-Rule:MF_01464};
GN Name=secF {ECO:0000255|HAMAP-Rule:MF_01464}; OrderedLocusNames=MJ1253;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
CC -!- FUNCTION: Involved in protein export. {ECO:0000255|HAMAP-
CC Rule:MF_01464}.
CC -!- SUBUNIT: Part of the protein translocation apparatus. Forms a complex
CC with SecD. {ECO:0000255|HAMAP-Rule:MF_01464}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01464};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01464}.
CC -!- SIMILARITY: Belongs to the SecD/SecF family. SecF subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01464}.
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DR EMBL; L77117; AAB99256.1; -; Genomic_DNA.
DR PIR; D64456; D64456.
DR RefSeq; WP_010870766.1; NC_000909.1.
DR AlphaFoldDB; Q58650; -.
DR SMR; Q58650; -.
DR STRING; 243232.MJ_1253; -.
DR EnsemblBacteria; AAB99256; AAB99256; MJ_1253.
DR GeneID; 1452151; -.
DR KEGG; mja:MJ_1253; -.
DR eggNOG; arCOG03054; Archaea.
DR HOGENOM; CLU_060478_0_0_2; -.
DR InParanoid; Q58650; -.
DR OMA; FMAIVVY; -.
DR OrthoDB; 63405at2157; -.
DR PhylomeDB; Q58650; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-UniRule.
DR GO; GO:0006605; P:protein targeting; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01464_A; SecF_A; 1.
DR InterPro; IPR022813; SecD/SecF_arch_bac.
DR InterPro; IPR022646; SecD/SecF_CS.
DR InterPro; IPR024921; SecF_arc.
DR PANTHER; PTHR30081; PTHR30081; 1.
DR Pfam; PF07549; Sec_GG; 1.
DR Pfam; PF02355; SecD_SecF; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Protein transport; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..282
FT /note="Protein-export membrane protein SecF"
FT /id="PRO_0000095991"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
SQ SEQUENCE 282 AA; 31029 MW; D2AC5859AEFC1079 CRC64;
MIKDYKVSIA IPIALLILSI LLIGFKGIPK SIDITGGTEI TIKVNENMDI TPLKESLNGI
AEVKKLESAD GYYIVIRCKN EDVDIVKQKI KEFFHVDSLD KLNYSEKTIG ATLSSKFFEE
GFKAVGFAFM FMAIVVYLYF RNPVPSGAII LSALSDIIMA LGAMSLLGIE LSSATIAALL
MVIGYSVDSD ILLTTRVLKR LTKSFDETVK EAMKTGLTMT LTTITAMLIL LIVVKLFIPV
ADILANIATV LILALIADII NTWLLNAGIL KYYITEYRAK KI