ID A0A3N3ZSY6_9MICC Unreviewed; 350 AA.
AC A0A3N3ZSY6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
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:ROZ64702.1};
GN ORFNames=EDL96_02360 {ECO:0000313|EMBL:ROZ64702.1};
OS Kocuria soli.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=2485125 {ECO:0000313|EMBL:ROZ64702.1, ECO:0000313|Proteomes:UP000270616};
RN [1] {ECO:0000313|EMBL:ROZ64702.1, ECO:0000313|Proteomes:UP000270616}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M5W7-7 {ECO:0000313|EMBL:ROZ64702.1,
RC ECO:0000313|Proteomes:UP000270616};
RA Tuo L.;
RT "Kocuria sp. M5W7-7, whole genome shotgun sequence.";
RL Submitted (OCT-2018) 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. 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:ROZ64702.1}.
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DR EMBL; RKMF01000002; ROZ64702.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N3ZSY6; -.
DR OrthoDB; 9774769at2; -.
DR Proteomes; UP000270616; 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; 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:UP000270616};
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 26..44
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 143..162
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 169..191
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 197..216
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 286..311
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT DOMAIN 116..311
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
FT REGION 319..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 350 AA; 36874 MW; 1101FC803131E6F0 CRC64;
MSRFADFGND LYSGRKSFPF VPRRRLWLSI AAVLVVISAL IPVVRGGFNL GIDFTGGSEF
VVSDVSDASV EPGEQAVADT GHDGQSTVTN IAPGTVRVQT EQLDDDKTLA VRDALVQAYD
VSEDQVASNF VGPTWGAGIS QQMIRGLAIF LGLTAIMMAL YFRTWKMSLA SMAGVFVTVA
LTVGTYSLIG FEVTPSAIIG FLTVLSYSLY DTVVVFDKVR ENTKGVLDGT APQPRAGKGF
SDQINLAANQ TLVRSINTSV VGLLPVGAIL FIGAALLGAG TLKDLALAQF VGIVWGTLAT
LFVATPVYAA LRGMEPAVRK QDREAADRAA RGDGPDRAVS GRGRSGASTA
//
