ID A0A024HD11_PSEKB Unreviewed; 305 AA.
AC A0A024HD11;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
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:CDF82397.1};
GN ORFNames=PKB_1032 {ECO:0000313|EMBL:CDF82397.1};
OS Pseudomonas knackmussii (strain DSM 6978 / LMG 23759 / B13).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1301098 {ECO:0000313|EMBL:CDF82397.1, ECO:0000313|Proteomes:UP000025241};
RN [1] {ECO:0000313|EMBL:CDF82397.1, ECO:0000313|Proteomes:UP000025241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B13 {ECO:0000313|EMBL:CDF82397.1,
RC ECO:0000313|Proteomes:UP000025241};
RA Linke B.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDF82397.1, ECO:0000313|Proteomes:UP000025241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B13 {ECO:0000313|EMBL:CDF82397.1,
RC ECO:0000313|Proteomes:UP000025241};
RA Miyazaki R., Bertelli C., Falquet L., Robinson-Rechavi M., Gharib W.,
RA Roy S., Van der Meer J.R.;
RT "Genome sequence of the 3-chlorobenzoate degrading bacterium Pseudomonas
RT knackmussii B13 shows multiple evidence for horizontal gene transfer.";
RL Submitted (MAY-2014) 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; HG322950; CDF82397.1; -; Genomic_DNA.
DR RefSeq; WP_043249559.1; NZ_HG322950.1.
DR AlphaFoldDB; A0A024HD11; -.
DR STRING; 1301098.PKB_1032; -.
DR KEGG; pkc:PKB_1032; -.
DR PATRIC; fig|1301098.3.peg.1043; -.
DR eggNOG; COG0341; Bacteria.
DR HOGENOM; CLU_050012_1_0_6; -.
DR OrthoDB; 9774769at2; -.
DR Proteomes; UP000025241; 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}; Reference proteome {ECO:0000313|Proteomes:UP000025241};
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 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 133..150
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 157..178
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 184..205
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 258..286
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT DOMAIN 112..287
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 305 AA; 33018 MW; 0FEF8732D51F754F CRC64;
MNIKIGTINF MGVRNIAFAC TLILSLIALG SWFTKGLNFG LDFTGGTLIE LSYQQPAELA
KVREQLEKAG YNEAVVQSFG DTKDVLVRMP SEDPELGKKV AGALQAADAA NPASLKRVEY
VGPQVGEELR DQGGLGMLLA LGGILVYVGF RFQWKFALGA ILSLIHDVII VMGVLSFFQI
TFDLTVLAAV LAVVGYSLND TIVIFDRVRE NFRVLRKASL IDNINISTSQ TLLRTMATSI
STLLAIAALL FFGGDNLFGF SIALFVGVLA GTYSSIYIAD VVLIWLKLSA EDLIPPATKE
VDDRP
//
