ID   SECF_HALVD              Reviewed;         287 AA.
AC   D4GTK4; Q8U4U0;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Protein-export membrane protein SecF;
GN   Name=secF; OrderedLocusNames=HVO_1975;
OS   Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS   NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=309800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN PROTEIN EXPORT, SUBUNIT,
RP   SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND PROBABLE OPERON STRUCTURE.
RC   STRAIN=DS2 / DS70, and DS2 / DSM 5716 / WFD11;
RX   PubMed=16452406; DOI=10.1128/jb.188.4.1251-1259.2006;
RA   Hand N.J., Klein R., Laskewitz A., Pohlschroder M.;
RT   "Archaeal and bacterial SecD and SecF homologs exhibit striking structural
RT   and functional conservation.";
RL   J. Bacteriol. 188:1251-1259(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC   B-1768 / DS2;
RX   PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA   Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA   Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA   Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT   "The complete genome sequence of Haloferax volcanii DS2, a model
RT   archaeon.";
RL   PLoS ONE 5:E9605-E9605(2010).
CC   -!- FUNCTION: Involved in protein export. {ECO:0000269|PubMed:16452406}.
CC   -!- SUBUNIT: Part of the protein translocation apparatus. Forms complexes
CC       with SecD. {ECO:0000269|PubMed:16452406}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16452406};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:16452406}.
CC   -!- DISRUPTION PHENOTYPE: A double secD and secF deletion grows very poorly
CC       on solid medium at 45 degrees Celsius, confers a severe cold-sensitive
CC       growth phenotype (30 degrees Celsius), as well as having defects in
CC       Sec-dependent protein translocation. Has no effects on Sec-independent
CC       Tat substrate protein export. {ECO:0000269|PubMed:16452406}.
CC   -!- SIMILARITY: Belongs to the SecD/SecF family. SecF subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF395892; AAL74408.1; -; Genomic_DNA.
DR   EMBL; CP001956; ADE04671.1; -; Genomic_DNA.
DR   RefSeq; WP_004041854.1; NC_013967.1.
DR   AlphaFoldDB; D4GTK4; -.
DR   SMR; D4GTK4; -.
DR   STRING; 309800.C498_05146; -.
DR   EnsemblBacteria; ADE04671; ADE04671; HVO_1975.
DR   GeneID; 8925104; -.
DR   KEGG; hvo:HVO_1975; -.
DR   eggNOG; arCOG03054; Archaea.
DR   HOGENOM; CLU_060478_0_0_2; -.
DR   OMA; DLMNTYL; -.
DR   OrthoDB; 63405at2157; -.
DR   Proteomes; UP000008243; 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   1: Evidence at protein level;
KW   Cell membrane; Membrane; Protein transport; Reference proteome;
KW   Translocation; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..287
FT                   /note="Protein-export membrane protein SecF"
FT                   /id="PRO_0000412203"
FT   TOPO_DOM        1..18
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        40..129
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        130..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        151..152
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        174..176
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        177..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        198..225
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        226..248
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        249..251
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        252..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        275..287
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   287 AA;  30425 MW;  16BD0AAEF49A9B19 CRC64;
     MVEFTVPEVD YTRYTNRQLA AVPLAVLAVA LLVIGGWYVA TGAPVNPGVD FTGGTELRIA
     TDAPQSEVAA AFDSQPESIR SVAADGTYVV TFQSGSATST ELQTQAEDAG FEVRSIDAVS
     ANFGGETQLL ALGGLAVAFA GMSVLVFAMF RSFVPSIAVV LSAFSDIVIP VALMNLFGIE
     LSLGTVAALL MLIGYSVDSD ILLNNHVLRR SGDFYESTAR AMRTGVTMTL TSIAAMIVMT
     IMATLFGIQL LAAIGTVLVF GLTADLMNTY MLNVTLLRWY KFEGVTR