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Database: UniProt
Entry: E7G460_9HELI
LinkDB: E7G460_9HELI
Original site: E7G460_9HELI 
ID   E7G460_9HELI            Unreviewed;       321 AA.
AC   E7G460;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, 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:0000256|HAMAP-Rule:MF_01464,
GN   ECO:0000313|EMBL:EFX41842.1};
GN   ORFNames=HSUHS5_0754 {ECO:0000313|EMBL:EFX41842.1};
OS   Helicobacter suis HS5.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=710394 {ECO:0000313|EMBL:EFX41842.1, ECO:0000313|Proteomes:UP000054093};
RN   [1] {ECO:0000313|EMBL:EFX41842.1, ECO:0000313|Proteomes:UP000054093}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS5 {ECO:0000313|EMBL:EFX41842.1,
RC   ECO:0000313|Proteomes:UP000054093};
RX   PubMed=21414191; DOI=10.1186/1297-9716-42-51;
RA   Vermoote M., Vandekerckhove T.T., Flahou B., Pasmans F., Smet A.,
RA   De Groote D., Van Criekinge W., Ducatelle R., Haesebrouck F.;
RT   "Genome sequence of Helicobacter suis supports its role in gastric
RT   pathology.";
RL   Vet. Res. 42:51-51(2011).
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:0000256|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: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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFX41842.1}.
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DR   EMBL; ADHO01000123; EFX41842.1; -; Genomic_DNA.
DR   RefSeq; WP_006564545.1; NZ_ADHO01000123.1.
DR   AlphaFoldDB; E7G460; -.
DR   GeneID; 56929175; -.
DR   Proteomes; UP000054093; Unassembled WGS sequence.
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   Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 1.
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; IPR048634; SecD_SecF_C.
DR   InterPro; IPR005665; SecF_bac.
DR   NCBIfam; TIGR00916; 2A0604s01; 1.
DR   NCBIfam; TIGR00966; transloc_SecF; 1.
DR   PANTHER; PTHR30081:SF8; PROTEIN TRANSLOCASE SUBUNIT SECF; 1.
DR   PANTHER; PTHR30081; PROTEIN-EXPORT MEMBRANE PROTEIN SEC; 1.
DR   Pfam; PF07549; Sec_GG; 1.
DR   Pfam; PF02355; SecD_SecF; 1.
DR   PRINTS; PR01755; SECFTRNLCASE.
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}; Reference proteome {ECO:0000313|Proteomes:UP000054093};
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        20..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   TRANSMEM        135..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   TRANSMEM        159..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   TRANSMEM        188..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   TRANSMEM        238..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   TRANSMEM        266..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   DOMAIN          109..289
FT                   /note="Protein export membrane protein SecD/SecF C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02355"
SQ   SEQUENCE   321 AA;  35813 MW;  08365AAD41004D55 CRC64;
     MELFKRVRIL NFMEYSKWGL GASCVVLLLC LALIIFKGFN LGVDFAGGSV AQVRFEKKAP
     LAQIREVFAK AHLNGVQVSA FGSDQEVVIK IPVGKQEIKD LGSQITEILA PLGKFEIRKL
     DSVGPKVGDE LKQRGILSLV LAIVAMMLYV SFRYEWRFAL ASILALVHDS LITATSAIVF
     NIDLNLEVIA AVLTLIGYSI NDTIIIFDRI REKMLAGRSN DLNFVINEAI SSTLTRTLLT
     SLTVFFVLLV LYLFGSRILI GFSLPMLIGT VVGTYSSIFL APRIAVLLGF DLAKYHDNEL
     KKAKRKQEKE RLRRLYEHGR V
//
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