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Database: UniProt
Entry: A0A0A0ECZ1_9RHOB
LinkDB: A0A0A0ECZ1_9RHOB
Original site: A0A0A0ECZ1_9RHOB 
ID   A0A0A0ECZ1_9RHOB        Unreviewed;       322 AA.
AC   A0A0A0ECZ1;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-SEP-2017, entry version 16.
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=ATO9_15210 {ECO:0000313|EMBL:KGM47943.1};
OS   Pseudooceanicola atlanticus.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Pseudooceanicola.
OX   NCBI_TaxID=1461694 {ECO:0000313|EMBL:KGM47943.1, ECO:0000313|Proteomes:UP000030004};
RN   [1] {ECO:0000313|EMBL:KGM47943.1, ECO:0000313|Proteomes:UP000030004}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=22II-s11g {ECO:0000313|EMBL:KGM47943.1,
RC   ECO:0000313|Proteomes:UP000030004};
RX   PubMed=25663028; DOI=10.1007/s10482-015-0398-2;
RA   Lai Q., Li G., Liu X., Du Y., Sun F., Shao Z.;
RT   "Pseudooceanicola atlanticus gen. nov. sp. nov., isolated from surface
RT   seawater of the Atlantic Ocean and reclassification of Oceanicola
RT   batsensis, Oceanicola marinus, Oceanicola nitratireducens, Oceanicola
RT   nanhaiensis, Oceanicola antarcticus and Oceanicola flagellatus, as
RT   Pseudooceanicola batsensis comb. nov., Pseudooceanicola marinus comb.
RT   nov., Pseudooceanicola nitratireducens comb. nov., Pseudooceanicola
RT   nanhaiensis comb. nov., Pseudooceanicola antarcticus comb. nov., and
RT   Pseudooceanicola flagellatus comb. nov.";
RL   Antonie Van Leeuwenhoek 107:1065-1074(2015).
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-YajC and YidC. {ECO:0000256|HAMAP-
CC       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:KGM47943.1}.
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DR   EMBL; AQQX01000006; KGM47943.1; -; Genomic_DNA.
DR   RefSeq; WP_043750818.1; NZ_AQQX01000006.1.
DR   EnsemblBacteria; KGM47943; KGM47943; ATO9_15210.
DR   Proteomes; UP000030004; 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:UP000030004};
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:UP000030004};
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     20     45       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    143    164       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    171    192       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    198    222       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    250    268       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    274    294       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
SQ   SEQUENCE   322 AA;  35126 MW;  3F4C34BE24C5E7FE CRC64;
     MRLRLVPQET KIDFFKSGRL ALILSAFMIV ASLAAEGIIG LNFGIDFRGG TTIRTESTEP
     VDIGVYRDSI SELGLGDVTI TEVFDPTFGP ERNVAMVRIQ AQDGEESVSA QMIADVEGAL
     QSVVPDIQFV SVESVGPKVS GELIQTAVIA VLLAIFAVLV YIWLRFEWQF AVGAVAALVH
     DVILTVGVFS VFQIRFDLAI IAALLTIVGY SLNDTVVVFD RVRENLRKYK KMELKELLNL
     SINETLSRTV MTSGTTLIAL IALIVLGGDV IRGFVFAMTW GVIVGTYSSV FIAGEILRRL
     GVKRDWSKPT DTTGNQFANI DA
//
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