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Database: UniProt
Entry: M0P8W3_9EURY
LinkDB: M0P8W3_9EURY
Original site: M0P8W3_9EURY 
ID   M0P8W3_9EURY            Unreviewed;       529 AA.
AC   M0P8W3;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Protein-export membrane protein SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   Name=secD {ECO:0000256|HAMAP-Rule:MF_01463,
GN   ECO:0000313|EMBL:EMA66471.1};
GN   ORFNames=C461_10538 {ECO:0000313|EMBL:EMA66471.1};
OS   Halorubrum aidingense JCM 13560.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Halorubraceae; Halorubrum.
OX   NCBI_TaxID=1230454 {ECO:0000313|EMBL:EMA66471.1, ECO:0000313|Proteomes:UP000011575};
RN   [1] {ECO:0000313|EMBL:EMA66471.1, ECO:0000313|Proteomes:UP000011575}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 13560 {ECO:0000313|EMBL:EMA66471.1,
RC   ECO:0000313|Proteomes:UP000011575};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
CC   -!- FUNCTION: Involved in protein export. {ECO:0000256|HAMAP-
CC       Rule:MF_01463}.
CC   -!- SUBUNIT: Part of the protein translocation apparatus. Forms a complex
CC       with SecF. {ECO:0000256|HAMAP-Rule:MF_01463}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01463};
CC       Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01463}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
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 of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01463}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EMA66471.1}.
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DR   EMBL; AOJI01000026; EMA66471.1; -; Genomic_DNA.
DR   RefSeq; WP_008001027.1; NZ_AOJI01000026.1.
DR   AlphaFoldDB; M0P8W3; -.
DR   STRING; 1230454.C461_10538; -.
DR   PATRIC; fig|1230454.4.peg.2122; -.
DR   OrthoDB; 146638at2157; -.
DR   Proteomes; UP000011575; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0006605; P:protein targeting; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.70.3220; -; 1.
DR   Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 1.
DR   HAMAP; MF_01463_A; SecD_A; 1.
DR   InterPro; IPR022813; SecD/SecF_arch_bac.
DR   InterPro; IPR024912; SecD_arc.
DR   InterPro; IPR048634; SecD_SecF_C.
DR   PANTHER; PTHR30081:SF8; PROTEIN TRANSLOCASE SUBUNIT SECF; 1.
DR   PANTHER; PTHR30081; PROTEIN-EXPORT MEMBRANE PROTEIN SEC; 1.
DR   Pfam; PF02355; SecD_SecF; 1.
DR   SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_01463};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01463};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927, ECO:0000256|HAMAP-
KW   Rule:MF_01463};
KW   Translocation {ECO:0000256|ARBA:ARBA00023010, ECO:0000256|HAMAP-
KW   Rule:MF_01463};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_01463};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_01463};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01463}.
FT   TRANSMEM        374..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        399..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        427..448
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        469..490
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        496..514
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   DOMAIN          360..512
FT                   /note="Protein export membrane protein SecD/SecF C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02355"
SQ   SEQUENCE   529 AA;  55885 MW;  471F5AD9C7360E8C CRC64;
     MLEPIKKNWR ILLLLVVVVA ASVALFAPQF GPETAPGENA SEAQQGITNL QYGLDLAGGT
     RVRAPLLGHT ATGVDFGGDQ PTDVAQNVAD ELDGVPVRDV GANAEEGAVE VTDSSVTESE
     FQAAMDASGY AYEDVRSGVT QETRDVAENV IQGKINEAGL SGGSVQQVQS ISGEYFILVE
     VPGQDRSDVI DLLEERGTVQ IDIAYPTDNG TEVQEAVLTQ DDFDEIGTAA ESERGPGAYV
     PVTVRNTASD GSQSPAHEFQ QAVVDRGFPS AYSSNAAQCD YGENPDDVSN PCLLLTVDGE
     VVNSFGMDSD LAASMDRGTW ADTGNFRLTT GEFESAQTIS INLRAGALPA ELDISGQGTS
     STISATQGEN FRTYSLITGI LAVFAVAGMV FLRYREPRVA LPMIVTALAE VYALLGFAAL
     VSYPLELAVI AGFIAVVGTG VDDLVIIADE VMSEGDVNSR KVFDSRFRRA FWVIGAAAAT
     TIIAMSPLMV LSLGDLSGFA IFTILGVLIG VLITRPAYGD ILRRLLTVR
//
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