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Database: UniProt
Entry: A0A086YP15_9FIRM
LinkDB: A0A086YP15_9FIRM
Original site: A0A086YP15_9FIRM 
ID   A0A086YP15_9FIRM        Unreviewed;       414 AA.
AC   A0A086YP15;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-SEP-2017, entry version 15.
DE   RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   ORFNames=DK28_0201370 {ECO:0000313|EMBL:KFD42014.1};
OS   Peptococcaceae bacterium SCADC1_2_3.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae.
OX   NCBI_TaxID=1487582 {ECO:0000313|EMBL:KFD42014.1, ECO:0000313|Proteomes:UP000027084};
RN   [1] {ECO:0000313|EMBL:KFD42014.1, ECO:0000313|Proteomes:UP000027084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCADC1_2_3 {ECO:0000313|EMBL:KFD42014.1};
RA   Tan B.F., Charchuk R., Li C., Nesbo C., Abu-Laban N., Foght J.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KFD42014.1, ECO:0000313|Proteomes:UP000027084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCADC1_2_3 {ECO:0000313|EMBL:KFD42014.1};
RA   Tan B., Charchuk R., Li C., Nesbo C., Abu-Laban N., Foght J.;
RT   "Draft genome sequence of an unculturable Firmicutes affiliated with
RT   Peptococcaceae sorted using a microfluidic device from methanogenic
RT   alkane-degrading cultures.";
RL   Submitted (JUL-2014) 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_01463, ECO:0000256|SAAS:SAAS00541769}.
CC   -!- SUBUNIT: Forms a complex with SecF. 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_01463}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01463}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01463}.
CC   -!- SIMILARITY: Belongs to the SecD/SecF family. SecD subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01463}.
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:KFD42014.1}.
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DR   EMBL; JJNX02000011; KFD42014.1; -; Genomic_DNA.
DR   EnsemblBacteria; KFD42014; KFD42014; DK28_0201370.
DR   Proteomes; UP000027084; 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_01463_B; SecD_B; 1.
DR   InterPro; IPR001036; Acrflvin-R.
DR   InterPro; IPR005791; SecD.
DR   InterPro; IPR022813; SecD/SecF_arch_bac.
DR   InterPro; IPR022645; SecD/SecF_bac.
DR   InterPro; IPR022646; SecD/SecF_CS.
DR   Pfam; PF07549; Sec_GG; 1.
DR   Pfam; PF02355; SecD_SecF; 1.
DR   PRINTS; PR00702; ACRIFLAVINRP.
DR   TIGRFAMs; TIGR00916; 2A0604s01; 1.
DR   TIGRFAMs; TIGR01129; secD; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00425060};
KW   Complete proteome {ECO:0000313|Proteomes:UP000027084};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00284057};
KW   Protein transport {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00425133};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027084};
KW   Translocation {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00425069};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00425065};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00425143};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00425109}.
FT   TRANSMEM      7     28       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    253    269       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    276    294       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    300    324       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    345    367       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    373    397       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
SQ   SEQUENCE   414 AA;  45225 MW;  438D01826DBF298C CRC64;
     MQKNKILQIA GLFAVIILAL LISFAPLFKS NEFLNKYLPL IKNINLGLDL RGGVHVVIEA
     KGPPEEITPE KMKQLRAVIE RRVDQFGVSE PVIQQQGSRR LIVELAGIKN PEEAVRNIVK
     VANLEFKTED GKTVITGADL KDARETKDPA SNQVKVDLTF TPMGARKFAE VTAANVNKTI
     GIYLDERLLQ NPVVKEAIPS GRAEISGYET LEEAHNIAIL LRSGALPVKV GIEEMRTVGP
     SLGADSLNKS QQAGLMGIIA ILFFMLMYYR LPGTVAVFAL IIYAIIVTLV FWGLKATMTL
     PGIAAFLLSL GMAVDTNIII FERFKEELRT GKSLRAAIDA GFKRGFAAVF DAQVTTLIAA
     VVLYFFGTGS IRGFALTLGI GILVSLFTAV TMTRWLLHLV VGSGLFKNLK YYGT
//
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