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Database: UniProt
Entry: A0A0W1S947_9GAMM
LinkDB: A0A0W1S947_9GAMM
Original site: A0A0W1S947_9GAMM 
ID   A0A0W1S947_9GAMM        Unreviewed;       617 AA.
AC   A0A0W1S947;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   25-APR-2018, entry version 11.
DE   RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   Name=secD {ECO:0000256|HAMAP-Rule:MF_01463,
GN   ECO:0000313|EMBL:KTG22627.1};
GN   ORFNames=AUR68_25840 {ECO:0000313|EMBL:KTG22627.1};
OS   Idiomarina sp. H105.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Idiomarina.
OX   NCBI_TaxID=1766622 {ECO:0000313|EMBL:KTG22627.1, ECO:0000313|Proteomes:UP000054149};
RN   [1] {ECO:0000313|EMBL:KTG22627.1, ECO:0000313|Proteomes:UP000054149}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H105 {ECO:0000313|EMBL:KTG22627.1,
RC   ECO:0000313|Proteomes:UP000054149};
RA   Zhang G., Stingl U., Rashid M.;
RT   "The draft genome sequence of Idiomarina sp., isolated from Erba
RT   brine-seawater interface of Red Sea.";
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_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-YajC and YidC. {ECO:0000256|HAMAP-
CC       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:KTG22627.1}.
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DR   EMBL; LOPZ01000224; KTG22627.1; -; Genomic_DNA.
DR   EnsemblBacteria; KTG22627; KTG22627; AUR68_25840.
DR   Proteomes; UP000054149; 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; IPR005791; SecD.
DR   InterPro; IPR027398; SecD-TM.
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; PF13721; SecD-TM1; 1.
DR   Pfam; PF02355; SecD_SecF; 1.
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:UP000054149};
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:UP000054149};
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     25       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    456    473       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    480    502       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    508    530       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    551    573       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    579    603       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   DOMAIN        2    103       SecD-TM1. {ECO:0000259|Pfam:PF13721}.
SQ   SEQUENCE   617 AA;  67520 MW;  3F35313A993259D5 CRC64;
     MLNRYPLWKY LLILVVLVVG LIYSLPNLFP ADPAIQVSDA QGNALDERQI TRVEEALSER
     DIAVKAVEEN NGQWLIRLQS DDDQLDARDI AAEVLGPNAT VALNLADATP GWLQAFSASP
     MTLGLDLRGG VHFLLEVDMD AALAQRLEVN ASAMRELLRS ERIRYRNTTI DGRSLSIDFA
     SSEDRDAARR LISRDFPNFE YTSEGDGRTS RLVMTLSDMA VNEIQDYAIN QNLTTLRNRV
     NELGVAEPMV QRQGPSQIVV ELPGVQDTVA AKRIVGATAN LEFRLEARHD TPDAETERFE
     FRNDPARSAE LMRDVIITGD SVSSASNSFD ENGRPQVNIN LDGTGGTLMN RATRTNIGRN
     MAVLFIEHKS EDRIEVDPET GEETIVREPY TERGLISLAT IQSALGNSFR ITGLDSPTEA
     AELALLLRSG SLAAPIYFVQ ERTIGPSLGA ENIERGLLSV QIGLLLVVLF MLVRYKVFGV
     FANIALALNL TLLVAVMSML GATLTLPGIA GIVLTLGMAV DANVLIFERI REELRNGMSI
     QQAIYAGYER AFTSIVDANI TTLLVAVILF SIGTGPVKGF AVTLSIGILT SMFTALLVTR
     AMVNLAYGGK HVKKLWI
//
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