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Database: UniProt
Entry: A0A0W7W8V0_9MICO
LinkDB: A0A0W7W8V0_9MICO
Original site: A0A0W7W8V0_9MICO 
ID   A0A0W7W8V0_9MICO        Unreviewed;       339 AA.
AC   A0A0W7W8V0;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-SEP-2017, entry version 9.
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=AUL38_01785 {ECO:0000313|EMBL:KUF07059.1};
OS   Leucobacter sp. G161.
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae;
OC   Leucobacter.
OX   NCBI_TaxID=663704 {ECO:0000313|EMBL:KUF07059.1, ECO:0000313|Proteomes:UP000053012};
RN   [1] {ECO:0000313|EMBL:KUF07059.1, ECO:0000313|Proteomes:UP000053012}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G161 {ECO:0000313|EMBL:KUF07059.1,
RC   ECO:0000313|Proteomes:UP000053012};
RA   Ge S., Dong X.;
RT   "High quality draft genome sequence of Leucobacter sp. G161, a
RT   distinct and effective chromium reducer.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Part of the Sec protein translocase complex. Interacts
CC       with the SecYEG preprotein conducting channel. SecDF uses the
CC       proton motive force (PMF) to complete protein translocation after
CC       the ATP-dependent function of SecA. {ECO:0000256|HAMAP-
CC       Rule:MF_01464, ECO:0000256|SAAS:SAAS00541769}.
CC   -!- SUBUNIT: Forms a complex with SecD. Part of the essential Sec
CC       protein translocation apparatus which comprises SecA, SecYEG and
CC       auxiliary proteins SecDF. Other proteins may also be involved.
CC       {ECO:0000256|HAMAP-Rule:MF_01464}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01464}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01464}.
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
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KUF07059.1}.
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DR   EMBL; LOHP01000060; KUF07059.1; -; Genomic_DNA.
DR   RefSeq; WP_059060921.1; NZ_LOHP01000060.1.
DR   EnsemblBacteria; KUF07059; KUF07059; AUL38_01785.
DR   Proteomes; UP000053012; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005622; C:intracellular; IEA:GOC.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015450; F:P-P-bond-hydrolysis-driven protein transmembrane transporter 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   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; IPR005665; SecF_bac.
DR   Pfam; PF07549; Sec_GG; 1.
DR   Pfam; PF02355; SecD_SecF; 1.
DR   PRINTS; PR01755; SECFTRNLCASE.
DR   TIGRFAMs; TIGR00916; 2A0604s01; 1.
DR   TIGRFAMs; TIGR00966; 3a0501s07; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00425060};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053012};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00284057};
KW   Protein transport {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00425133};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053012};
KW   Translocation {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00425069};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00425065};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00425143};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00425109}.
FT   TRANSMEM     27     45       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    146    165       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    172    192       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    198    219       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    257    276       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    282    308       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
SQ   SEQUENCE   339 AA;  36270 MW;  A0C288EBC45C6F4F CRC64;
     MARSFAELGN ALYTGEKSID FVGKRKIWYA VSALLIIIAI AGPFLRGGFQ LGIEFTGGSQ
     FQVHVSNSAD RDPAVAEQAV AEALPGSAPR ISVLGQNEVR VQTEALDDAQ NKAVTEALAA
     GYGIDADEVT YSFIGPVWGQ DITKQALIAL VVFILLAALV MAIYFRTWKM SLAAMLALFH
     DLIITAGIYG LAGFEVTPAA MIGFLTILGY SLYDTVVVFD KIRENTSPGE LSDLRTYGEA
     VNLAVNQTLV RSINTSVVAL LPVASILFVG AGFLGAGTLR DISLALFIGI IAGAYSTIFV
     SAPAYAHLRA GEKEIQERDE RILRQRAKQD ETEVVAATT
//
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