SECD_SALCH
ID SECD_SALCH Reviewed; 615 AA.
AC Q9ZFF8; Q57SF6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Protein translocase subunit SecD {ECO:0000255|HAMAP-Rule:MF_01463};
GN Name=secD {ECO:0000255|HAMAP-Rule:MF_01463}; OrderedLocusNames=SCH_0449;
OS Salmonella choleraesuis (strain SC-B67).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=321314;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kuhn F.C., Gies A.J., Smeltzer M., Crupper S.S., Sobieski R.J.;
RT "Identification of secD gene from Salmonella choleraesuis.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC-B67;
RX PubMed=15781495; DOI=10.1093/nar/gki297;
RA Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA Lee Y.-S.;
RT "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT invasive and resistant zoonotic pathogen.";
RL Nucleic Acids Res. 33:1690-1698(2005).
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-YajC and YidC. {ECO:0000255|HAMAP-Rule:MF_01463}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the SecD/SecF family. SecD subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01463}.
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DR EMBL; AF100611; AAC83834.1; -; Genomic_DNA.
DR EMBL; AE017220; AAX64355.1; -; Genomic_DNA.
DR RefSeq; WP_000934811.1; NC_006905.1.
DR AlphaFoldDB; Q9ZFF8; -.
DR SMR; Q9ZFF8; -.
DR PRIDE; Q9ZFF8; -.
DR EnsemblBacteria; AAX64355; AAX64355; SCH_0449.
DR KEGG; sec:SCH_0449; -.
DR HOGENOM; CLU_007894_4_3_6; -.
DR OMA; MVVYYRL; -.
DR Proteomes; UP000000538; 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: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 PANTHER; PTHR30081; PTHR30081; 1.
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 inner membrane; Cell membrane; Membrane; Protein transport;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..615
FT /note="Protein translocase subunit SecD"
FT /id="PRO_0000095969"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 477..497
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 504..524
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 546..568
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 585..605
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT CONFLICT 611
FT /note="T -> K (in Ref. 1; AAC83834)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 615 AA; 66605 MW; 81370B11FD5983F9 CRC64;
MLNRYPLWKY IMLVVVIIVG LLYALPNLYG EDPAVQITGV RGVAASEQTL IQVQKTLQEE
KIPAKSVALE EGAILARFDT TDTQLRAREA LMSVLGDKYV VALNLAPATP RWLAAIHADP
MKLGLDLRGG VHFLMEVDMD TALGKLQEQN IDSLRSDLRE KGIPYTTVRK ENNYGLSITF
RDSKARDEAI AYLTPRHRDL VISSQSGNQL RAVMTDARLS EAREYAVQQN INILRNRVNQ
LGVAEPVVQR QGADRIVVEL PGIQDTARAK EILGATATLE FRLVNTNVDQ AAAAAGRVPG
DSEVKQTREG QPVVLYKRVI LTGDHITDST SSQDEYNQPQ VNISLDSAGG NIMSNFTKDN
IGKPMATLFV EYKDSGKKDA NGRAVLVKQE EVINIANIQS RLGNSFRITG ISNPNEARQL
SLLLRAGALI APIQIVEERT IGPTLGMQNI KQGLEACLAG LVVSILFMIF FYKKFGLIAT
SALVANLVLI VGIMSLLPGA TLSMPGIAGI VLTLAVAVDA NVLINERIKE ELSNGRTVQQ
AINEGYAGAF SSIFDANITT LIKVIILYAV GTGAIKGFAI TTGIGVATSM FTAIIGTRAI
VNLLYGGKRV TKLSI