ID M0M4E5_9EURY Unreviewed; 545 AA.
AC M0M4E5;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 27.
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:EMA40682.1};
GN ORFNames=C447_04151 {ECO:0000313|EMBL:EMA40682.1};
OS Halococcus hamelinensis 100A6.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halococcaceae; Halococcus.
OX NCBI_TaxID=1132509 {ECO:0000313|EMBL:EMA40682.1, ECO:0000313|Proteomes:UP000011566};
RN [1] {ECO:0000313|EMBL:EMA40682.1, ECO:0000313|Proteomes:UP000011566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=100A6 {ECO:0000313|EMBL:EMA40682.1,
RC ECO:0000313|Proteomes:UP000011566};
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:EMA40682.1}.
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; AOMB01000010; EMA40682.1; -; Genomic_DNA.
DR RefSeq; WP_007691204.1; NZ_AOMB01000010.1.
DR AlphaFoldDB; M0M4E5; -.
DR PATRIC; fig|1132509.6.peg.966; -.
DR eggNOG; arCOG03055; Archaea.
DR OrthoDB; 146638at2157; -.
DR Proteomes; UP000011566; 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; 3.30.1360.200; -; 1.
DR Gene3D; 3.30.70.3400; -; 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}; Reference proteome {ECO:0000313|Proteomes:UP000011566};
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 390..409
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 416..441
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 447..465
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 486..506
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 512..530
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 376..528
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 545 AA; 56962 MW; 60E81972E6727C3C CRC64;
MIRDNWRIVL LVVFVVVAGL ALFVPGFGVD DGGNATATNA TSGPTNLQFG LELSGGTRIR
APLVGLTAEN VNVPPNQQAN LTGSVAEDLG VSPTDVQVRV GNESATVEVF SENVSQGQFA
SALQRAGYNT TRDDIRTGVT EETDESAVEV LENKISESGL TGGTVQTVSS GDQSYIQIEV
PNQNRSEVRD LVADQGQVQT VAYFTVEGNR TPSYCEGPVG GNGSGGGGGE GGANTCNVTV
LQSQDGFQSV GTVQRDQQGQ PIVPVTLTEQ AARPFTQAMQ RYGFADAANA SSRQGQVRTC
NFETGGGGHC LLTVRDGEVV YAASVTQGLA RQFATGSFVN DPGYQTSAGN ASEAQNLQVD
LQAGALPAPL NFDQGTSQYI LPSVAQRFKG LSLVTGLVAV LAVAGVVFVR YRELRVAIPM
VITALAEVFI LLGFSSAVGL ALDLSHIAGF IAVIGTGVDD LVIIADEILQ SEVKTGRVFQ
SRFRRAFWVI GAAAATTIIA MSPLAVLSLG DLRGFAIVTI VGVLIGVLIT RPAYGNVLRR
LLTDT
//