SECF_VIBAL
ID SECF_VIBAL Reviewed; 315 AA.
AC E9RGS4;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=Protein translocase subunit SecF;
GN Name=secF;
OS Vibrio alginolyticus.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=663;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=138-2;
RA Tsukazaki T., Mori H., Echizen Y., Ishitani R., Fukai S., Tanaka T.,
RA Sasaki Y., Mio K., Kuwata M., Perederina A., Vassylyev D.G., Kohno T.,
RA Sato C., Maturana A., Ito K., Nureki O.;
RT "Structure and function of SecDF, a protein export-enhancing membrane
RT component.";
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION IN E.COLI, AND FUNCTION IN PROTEIN TRANSLOCATION.
RC STRAIN=138-2;
RX PubMed=21562494; DOI=10.1038/nature09980;
RA Tsukazaki T., Mori H., Echizen Y., Ishitani R., Fukai S., Tanaka T.,
RA Perederina A., Vassylyev D.G., Kohno T., Maturana A.D., Ito K., Nureki O.;
RT "Structure and function of a membrane component SecDF that enhances protein
RT export.";
RL Nature 474:235-238(2011).
CC -!- FUNCTION: Expression of V.alginolyticus SecDF in an E.coli secDF mutant
CC restores protein export in a Na(+)-dependent manner, strongly
CC suggesting SecDF functions via cation-coupled protein translocation.
CC {ECO:0000269|PubMed:21562494}.
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 (By similarity). {ECO:0000250}.
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-YajC and YidC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SecD/SecF family. SecF subfamily.
CC {ECO:0000305}.
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DR EMBL; AB583187; BAJ78590.1; -; Genomic_DNA.
DR RefSeq; WP_005391572.1; NZ_PZOD01000080.1.
DR AlphaFoldDB; E9RGS4; -.
DR SMR; E9RGS4; -.
DR STRING; 663.BAU10_01935; -.
DR eggNOG; COG0341; Bacteria.
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 1: Evidence at protein level;
KW Cell membrane; Membrane; Protein transport; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..315
FT /note="Protein translocase subunit SecF"
FT /id="PRO_0000412707"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 315 AA; 34414 MW; 0709588543202498 CRC64;
MFQILKAEKT IGFMRWSKVA FVFSIFMIAA SIFTLSTKWL NWGLDFTGGT LIEVGFEKPA
NLEKIRTALD AKGFGDATVQ NFGSAREVMV RLRPRDDVSG ETLGNQIIGA IKDGTGESVE
MRRIEFVGPN VGDELTEAGG LAILVSLICI LLYVSMRFEW RLAAGAVMAL AHDIIITLGV
FSFLQIEVDL TIVAALLTVV GYSLNDTIVV FDRIRENFRK MRKGEPADIM DASITQTLSR
TLITSGTTLF VVIALFMQGG AMIHGFATAL LLGITVGTYS SIYVASALAL KLGIQKEHLM
PPQVEKEGAE FDEMP