SECF_ELUMP
ID SECF_ELUMP Reviewed; 321 AA.
AC B2KBZ0;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Protein translocase subunit SecF;
GN Name=secF {ECO:0000255|HAMAP-Rule:MF_01464}; OrderedLocusNames=Emin_0562;
OS Elusimicrobium minutum (strain Pei191).
OC Bacteria; Elusimicrobia; Elusimicrobia; Elusimicrobiales;
OC Elusimicrobiaceae; Elusimicrobium.
OX NCBI_TaxID=445932;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pei191;
RX PubMed=19270133; DOI=10.1128/aem.02698-08;
RA Herlemann D.P.R., Geissinger O., Ikeda-Ohtsubo W., Kunin V., Sun H.,
RA Lapidus A., Hugenholtz P., Brune A.;
RT "Genomic analysis of 'Elusimicrobium minutum,' the first cultivated
RT representative of the phylum 'Elusimicrobia' (formerly termite group 1).";
RL Appl. Environ. Microbiol. 75:2841-2849(2009).
CC -!- FUNCTION: Part of the Sec protein translocase complex. Interacts with
CC the SecYEG preprotein conducting channel. SecDF uses the proton motive
CC force (PMF) to complete protein translocation after the ATP-dependent
CC function of SecA. {ECO:0000255|HAMAP-Rule:MF_01464}.
CC -!- SUBUNIT: Forms a complex with SecD. Part of the essential Sec protein
CC translocation apparatus which comprises SecA, SecYEG and auxiliary
CC proteins SecDF. Other proteins may also be involved.
CC {ECO:0000255|HAMAP-Rule:MF_01464}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01464}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC 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; CP001055; ACC98117.1; -; Genomic_DNA.
DR RefSeq; WP_012414732.1; NC_010644.1.
DR AlphaFoldDB; B2KBZ0; -.
DR SMR; B2KBZ0; -.
DR STRING; 445932.Emin_0562; -.
DR EnsemblBacteria; ACC98117; ACC98117; Emin_0562.
DR KEGG; emi:Emin_0562; -.
DR HOGENOM; CLU_050012_0_1_0; -.
DR OMA; AFEWRMA; -.
DR OrthoDB; 410730at2; -.
DR Proteomes; UP000001029; 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:0015450; F:protein-transporting ATPase activity; IEA:InterPro.
DR GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-UniRule.
DR GO; GO:0006605; P:protein targeting; IEA:UniProtKB-UniRule.
DR GO; GO:0043952; P:protein transport by the Sec complex; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01464_B; SecF_B; 1.
DR InterPro; IPR022813; SecD/SecF_arch_bac.
DR InterPro; IPR022645; SecD/SecF_bac.
DR InterPro; IPR022646; SecD/SecF_CS.
DR InterPro; IPR005665; SecF_bac.
DR PANTHER; PTHR30081; PTHR30081; 1.
DR Pfam; PF07549; Sec_GG; 1.
DR Pfam; PF02355; SecD_SecF; 1.
DR PRINTS; PR01755; SECFTRNLCASE.
DR TIGRFAMs; TIGR00916; 2A0604s01; 1.
DR TIGRFAMs; TIGR00966; 3a0501s07; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Protein transport;
KW Reference proteome; Translocation; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..321
FT /note="Protein translocase subunit SecF"
FT /id="PRO_0000412695"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
SQ SEQUENCE 321 AA; 35877 MW; 175242B311A1CD43 CRC64;
MMNLIPKTNF DFLKIRKYFY AVSAIILIAG LICILTRGLN MGIDFKGGTM VQVQFTESIT
IDQVRSAVEK YNPEIQSYVG KNTYMIKIKG SQENVNEVRS DVETSLTAAK LKFTVVATDF
VGPTVGKDLG ERALWALALS LVFMVLYIAF RFQNIIWGTA GVIALIHDAF FMVAAFAFLQ
KEFDLVIVAA LLTAVGYSIN DNIVIFDRMR ENIKENPKES FYNIVNRSLN ETLSRTVITG
STVLIVLVII YFFGGEVLKN FSLIMLIGVI VGTYSTLFIA TPIVYDWAKD SDNFAKTVGN
QDVALAAEIK TAKKHNKKKH R