GenomeNet

Database: UniProt
Entry: A0A0S9R1P7_9ACTN
LinkDB: A0A0S9R1P7_9ACTN
Original site: A0A0S9R1P7_9ACTN 
ID   A0A0S9R1P7_9ACTN        Unreviewed;       562 AA.
AC   A0A0S9R1P7;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   18-JUL-2018, entry version 10.
DE   RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   ORFNames=ASF37_14335 {ECO:0000313|EMBL:KQP76105.1};
OS   Aeromicrobium sp. Leaf289.
OC   Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC   Aeromicrobium.
OX   NCBI_TaxID=1736324 {ECO:0000313|EMBL:KQP76105.1, ECO:0000313|Proteomes:UP000051640};
RN   [1] {ECO:0000313|EMBL:KQP76105.1, ECO:0000313|Proteomes:UP000051640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf289 {ECO:0000313|EMBL:KQP76105.1,
RC   ECO:0000313|Proteomes:UP000051640};
RA   Millard Andrew;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQP76105.1, ECO:0000313|Proteomes:UP000051640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf289 {ECO:0000313|EMBL:KQP76105.1,
RC   ECO:0000313|Proteomes:UP000051640};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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_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: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {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:KQP76105.1}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; LMNK01000004; KQP76105.1; -; Genomic_DNA.
DR   RefSeq; WP_056555058.1; NZ_LMNK01000004.1.
DR   EnsemblBacteria; KQP76105; KQP76105; ASF37_14335.
DR   Proteomes; UP000051640; 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:UP000051640};
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   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    357    375       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    382    402       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    414    433       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    461    480       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    486    504       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
SQ   SEQUENCE   562 AA;  58786 MW;  E2FE3DF40C78E615 CRC64;
     MARPAPRPGR STAGIPRPRR TLLLFLALLL ALFGLLAGLD LKDGGGVWKP RLGLDLQGGT
     RITLQAEASS GDVTQAKLQE ARDIIDQRVN ATGVSEAEVS TQGGNQVVIE IPGQRKGNIV
     DEVGRTAQLR FRLLWGSGQS AAQAPDQKAV AAAAKTVSAA DWSKLSLDQL IAAETQGLDS
     LPKDYASAAE ALQTELAGFR CTKDDLAVDD VPDEPIVSCD PSTGETMILS PTVIEGTQVK
     SADAVVPQGS VEWVVAIELR KAGTEAFDAI TDALYQQEQA GNQAASRFAI VLDGEVLSAP
     TTNGHFTNGS SQISGGFTQS TSQSLANQLK YGALPLTFEV NGVSVEGPSL AGSQLEAGIV
     AGAIGLVLVM AYLLLYYRAL GLVAIGSLLV AGASTYAMVL LLGKSLGFTL TLPGIAGLIV
     AIGITADSFI VLFERIRDEV RDGKSLRLAV ESGWERARRT ILAADGVSLL AAVILFIFAI
     GVVRGFAFAL GLTTVIDVIV VFLFTKPLMS LLARTTFFGR GHKLSGFDAA HLGIGDRAVD
     RTGPVRRPDR APTPGSTTGG RS
//
DBGET integrated database retrieval system