ID H3R9E1_PANSE Unreviewed; 322 AA.
AC H3R9E1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 53.
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:EHU01804.1};
GN ORFNames=CKS_0250 {ECO:0000313|EMBL:EHU01804.1}, DSJ_19320
GN {ECO:0000313|EMBL:ARF51253.1};
OS Pantoea stewartii subsp. stewartii DC283.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=660596 {ECO:0000313|EMBL:EHU01804.1, ECO:0000313|Proteomes:UP000005050};
RN [1] {ECO:0000313|EMBL:EHU01804.1, ECO:0000313|Proteomes:UP000005050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DC283 {ECO:0000313|EMBL:EHU01804.1,
RC ECO:0000313|Proteomes:UP000005050};
RX PubMed=22111898; DOI=10.1111/j.1365-2958.2011.07926.x;
RA Wang X., Yang F., von Bodman S.B.;
RT "The genetic and structural basis of two distinct terminal side branch
RT residues in stewartan and amylovoran exopolysaccharides and their potential
RT role in host adaptation.";
RL Mol. Microbiol. 83:195-207(2012).
RN [2] {ECO:0000313|EMBL:EHU01804.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DC283 {ECO:0000313|EMBL:EHU01804.1};
RA Biehl B.S., Ding Y., Dugan-Rocha S.P., Gibbs R.A., Glasner J.D., Kovar C.,
RA Muzny D.M., Neeno-Eckwall E.C., Perna N.T., Qin X., von Bodman S.B.,
RA Weinstock G.M.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ARF51253.1, ECO:0000313|Proteomes:UP000192380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DC283 {ECO:0000313|EMBL:ARF51253.1,
RC ECO:0000313|Proteomes:UP000192380};
RA Duong D.A., Stevens A.M., Jensen R.V.;
RT "Complete Genome Assembly of Pantoea stewartii subsp. stewartii DC283, a
RT Corn Pathogen.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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-YajC and YidC. {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; CP017581; ARF51253.1; -; Genomic_DNA.
DR EMBL; AHIE01000002; EHU01804.1; -; Genomic_DNA.
DR RefSeq; WP_006117989.1; NZ_CP017581.1.
DR AlphaFoldDB; H3R9E1; -.
DR STRING; 660596.DSJ_19320; -.
DR GeneID; 61254321; -.
DR KEGG; pstw:DSJ_19320; -.
DR PATRIC; fig|660596.6.peg.484; -.
DR eggNOG; COG0341; Bacteria.
DR OrthoDB; 9774769at2; -.
DR Proteomes; UP000005050; Unassembled WGS sequence.
DR Proteomes; UP000192380; 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; 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};
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 24..43
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 168..190
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 274..296
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT DOMAIN 116..300
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 322 AA; 34959 MW; 17AAA47834A3AFB8 CRC64;
MAQEYNIEQL NHGRKVVDFM RWDTLAFIIS GLLIIISIAI VGVRGFNWGL DFTGGTVIEI
NLEKPADLDA IRGALVKSGF QEPLIQNFGS SRDVMVRMPP VTGPAGTELG NKVVTVINQT
TQQNATVKRI EFVGPSVGSD LAQAGALALL SALIAILIYI GIRFEWRLAL GTVLALAHDV
IITCGLLSLF RVEIDLTIVA SLMSVIGYSL NDKIVVSDRI RENFRKIRRG SSYDITNVSL
TQTLSRTLIT SLTTLAMILI LFIFGGALLK GFSLTMLIGV TIGTVSSIYV SSALALKLGM
KREHMLVQKV EKEGADQPSI LP
//
