ID Q649P2_9ARCH Unreviewed; 322 AA.
AC Q649P2;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Protein-export membrane protein SecF {ECO:0000256|HAMAP-Rule:MF_01464};
GN Name=SecF {ECO:0000313|EMBL:AAU83885.1};
GN Synonyms=secF {ECO:0000256|HAMAP-Rule:MF_01464};
GN ORFNames=GZ34H9_3 {ECO:0000313|EMBL:AAU83885.1};
OS uncultured archaeon GZfos34H9.
OC Archaea; environmental samples.
OX NCBI_TaxID=285375 {ECO:0000313|EMBL:AAU83885.1};
RN [1] {ECO:0000313|EMBL:AAU83885.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15353801; DOI=10.1126/science.1100025;
RA Hallam S.J., Putnam N., Preston C.M., Detter J.C., Rokhsar D.,
RA Richardson P.M., DeLong E.F.;
RT "Reverse methanogenesis: testing the hypothesis with environmental
RT genomics.";
RL Science 305:1457-1462(2004).
RN [2] {ECO:0000313|EMBL:AAU83885.1}
RP NUCLEOTIDE SEQUENCE.
RA Putnam N., Detter J.C., Richardson P.M., Rokhsar D.;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in protein export. {ECO:0000256|HAMAP-
CC Rule:MF_01464}.
CC -!- SUBUNIT: Part of the protein translocation apparatus. Forms a complex
CC with SecD. {ECO:0000256|HAMAP-Rule:MF_01464}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01464};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01464}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the SecD/SecF family. SecF subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01464}.
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DR EMBL; AY714862; AAU83885.1; -; Genomic_DNA.
DR AlphaFoldDB; Q649P2; -.
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 Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 1.
DR HAMAP; MF_01464_A; SecF_A; 1.
DR InterPro; IPR022813; SecD/SecF_arch_bac.
DR InterPro; IPR048634; SecD_SecF_C.
DR InterPro; IPR024921; SecF_arc.
DR PANTHER; PTHR30081; PROTEIN-EXPORT MEMBRANE PROTEIN SEC; 1.
DR PANTHER; PTHR30081:SF11; PROTEIN-EXPORT MEMBRANE PROTEIN SECF; 1.
DR Pfam; PF02355; SecD_SecF; 1.
DR SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01464};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01464};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927, ECO:0000256|HAMAP-
KW Rule:MF_01464};
KW Translocation {ECO:0000256|ARBA:ARBA00023010, ECO:0000256|HAMAP-
KW Rule:MF_01464};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01464};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01464};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01464}.
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 137..156
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 230..256
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 268..295
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT DOMAIN 119..296
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 322 AA; 35507 MW; 7285C31D8E6BFCEF CRC64;
MSEKESFLDK IDITKYSAKK LIAIPLILLL LAFVVIAYTQ MSVGSPVHLG MDFTGGTWVK
ISTDETKEAL AAKFDSYPVI LVGETGVGNE KRIEFDLTSD SLEYDRLIGT LNNEYGVGTY
ELESISAQFG LQYQTQALKA IIFAFIFMAI VVFVAFRMII PPLAVIFAAF SDIVVAIACM
NLIGMELSLG TVAALLMLIG YSVDSNILLT TNLLRKKGDL DVKIRKAMKT GITMTFTTLS
AVFAMFIVSS SIHLFSSHFA PIPILVDISL VLLFGLVMDL ANTWLLNAGI LKLYLEKKES
KKFKRKKGVE KLNVKKKSKN AI
//