SECD_THEYD
ID SECD_THEYD Reviewed; 540 AA.
AC B5YIG9;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Protein translocase subunit SecD {ECO:0000255|HAMAP-Rule:MF_01463};
GN Name=secD {ECO:0000255|HAMAP-Rule:MF_01463}; OrderedLocusNames=THEYE_A0280;
OS Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87).
OC Bacteria; Nitrospirae; Thermodesulfovibrionia; Thermodesulfovibrionales;
OC Thermodesulfovibrionaceae; Thermodesulfovibrio.
OX NCBI_TaxID=289376;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51303 / DSM 11347 / YP87;
RA Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT "The complete genome sequence of Thermodesulfovibrio yellowstonii strain
RT ATCC 51303 / DSM 11347 / YP87.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Part of the Sec protein translocase complex. Interacts with
CC the SecYEG preprotein conducting channel. SecDF uses the proton motive
CC force (PMF) to complete protein translocation after the ATP-dependent
CC function of SecA. {ECO:0000255|HAMAP-Rule:MF_01463}.
CC -!- SUBUNIT: Forms a complex with SecF. Part of the essential Sec protein
CC translocation apparatus which comprises SecA, SecYEG and auxiliary
CC proteins SecDF. Other proteins may also be involved.
CC {ECO:0000255|HAMAP-Rule:MF_01463}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01463}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01463}.
CC -!- SIMILARITY: Belongs to the SecD/SecF family. SecD subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01463}.
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DR EMBL; CP001147; ACI21654.1; -; Genomic_DNA.
DR RefSeq; WP_012546364.1; NC_011296.1.
DR RefSeq; YP_002248128.1; NC_011296.1.
DR AlphaFoldDB; B5YIG9; -.
DR SMR; B5YIG9; -.
DR STRING; 289376.THEYE_A0280; -.
DR EnsemblBacteria; ACI21654; ACI21654; THEYE_A0280.
DR KEGG; tye:THEYE_A0280; -.
DR PATRIC; fig|289376.4.peg.276; -.
DR eggNOG; COG0342; Bacteria.
DR HOGENOM; CLU_007894_4_3_0; -.
DR InParanoid; B5YIG9; -.
DR OMA; MVVYYRL; -.
DR OrthoDB; 121331at2; -.
DR Proteomes; UP000000718; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015450; F:protein-transporting ATPase 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:0015031; P:protein transport; IBA:GO_Central.
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 PANTHER; PTHR30081; PTHR30081; 1.
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 inner membrane; Cell membrane; Membrane; Protein transport;
KW Reference proteome; Translocation; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..540
FT /note="Protein translocase subunit SecD"
FT /id="PRO_0000412683"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 430..450
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 475..495
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 502..522
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
SQ SEQUENCE 540 AA; 59655 MW; E86EE1740A0D54DD CRC64;
MRKGIYLRIA LIAFTVILAI IFFLPNTPLF SYMPGWWKKN LPHKGIVLGL DLRGGSHLIF
EVDLKRAREI TVERIGMHLQ SLLEKKGLKP SVKVQGEKIF IQPVNEDVKK IIKENYADLS
ISEHGGNIIC ELPETAFKRV ETTSVEQAIE VIRNRIDQLG VAEPAIHKQG ENEIVVQLPG
VKDPKKALEI IGKTAQLEFK LLDEETTLWK QLPSLIKAGE EDTFLNQWKS KLPESDEIVF
QKIVNKETGE VYKRPYIVKK DVLLTGDLLA EAHVSIDQRF NEPYVSLRFN DAGAKIFEDI
TGKYVKRRLA IILDGNLYSA PVIQEKIEGG NAQISGSFTL EEAKDLAIVL RAGALPAPVK
LIQNVTVGPT LGKDSIEAGK MAVIIASIFV SLFMIIYYRL SGVIADFALI LNIILLIGAL
AALNATLTLP GIAGIALAVG MAVDSNVLMF ERIREELRLG KTPKAAIETG YKKAFWTIFD
SHVTTLITAA VLFHFGSGPI KGFAVTLSLG VAINLFTALI GTKTVFDFIY IGKERKSLSI