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Database: UniProt
Entry: A0A0U2VVA6_9BACL
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ID   A0A0U2VVA6_9BACL        Unreviewed;       312 AA.
AC   A0A0U2VVA6;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Protein-export membrane protein SecF {ECO:0000256|HAMAP-Rule:MF_01464};
GN   Name=secF {ECO:0000256|HAMAP-Rule:MF_01464};
GN   ORFNames=IJ21_16250 {ECO:0000313|EMBL:ALS27027.1};
OS   Paenibacillus sp. 32O-W.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1695218 {ECO:0000313|EMBL:ALS27027.1, ECO:0000313|Proteomes:UP000059673};
RN   [1] {ECO:0000313|Proteomes:UP000059673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=32O-W {ECO:0000313|Proteomes:UP000059673};
RA   Butler R.III., Wang J., Stark B.C., Pombert J.-F.;
RT   "Complete genome sequences of two moderately thermophilic Paenibacillus
RT   species.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ALS27027.1, ECO:0000313|Proteomes:UP000059673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=32O-W {ECO:0000313|EMBL:ALS27027.1,
RC   ECO:0000313|Proteomes:UP000059673};
RX   PubMed=26868401;
RA   Butler R.R.III., Wang J., Stark B.C., Pombert J.F.;
RT   "Complete Genome Sequences of Two Interactive Moderate Thermophiles,
RT   Paenibacillus napthalenovorans 32O-Y and Paenibacillus sp. 32O-W.";
RL   Genome Announc. 4:e01717-15(2016).
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}.
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DR   EMBL; CP013653; ALS27027.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0U2VVA6; -.
DR   STRING; 1695218.IJ21_16250; -.
DR   KEGG; pow:IJ21_16250; -.
DR   PATRIC; fig|1695218.3.peg.1725; -.
DR   OrthoDB; 9805019at2; -.
DR   Proteomes; UP000059673; Chromosome.
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; 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; 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:UP000059673};
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..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   TRANSMEM        135..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   TRANSMEM        163..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   TRANSMEM        190..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   TRANSMEM        245..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   TRANSMEM        274..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   DOMAIN          112..297
FT                   /note="Protein export membrane protein SecD/SecF C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02355"
SQ   SEQUENCE   312 AA;  35149 MW;  289E4839A4AD71E2 CRC64;
     MNYNTKYQTK IRFDFVRNRK KFFAFSIALT IAGILSLLIF NLNYGVDFKA GTNMDISLSG
     SSITQDEAKQ LLAEAGYEDV TPTVGGNRGE RVTVRFETVL EQSETNHIMK LFKDKYGEDV
     SSEINIVSPD MARELGIKTI FAIIIASVAI MLYVMLRFEW RMALAMNIAI LYDAFVVVAI
     FSIFRLQVDL PFIAAVLTTI GYSINDKIVI FDRIRENMRF NKVKNFDQLA ELVNASIWQT
     MARNIYTVLT VVIVAVCLFL FGSESIRLFS LAKIIGLLSG AYSTICIASQ LWLVMKNKQK
     PNKQAVKAQS AS
//
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