SECD_SHIFL
ID SECD_SHIFL Reviewed; 615 AA.
AC P0AG92; P19673; P72348; P77531;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Protein translocase subunit SecD {ECO:0000255|HAMAP-Rule:MF_01463};
GN Name=secD {ECO:0000255|HAMAP-Rule:MF_01463};
GN OrderedLocusNames=SF0345, S0353;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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 {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; AE005674; AAN42003.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP15880.1; -; Genomic_DNA.
DR RefSeq; NP_706296.1; NC_004337.2.
DR RefSeq; WP_000934822.1; NZ_WPGN01000028.1.
DR AlphaFoldDB; P0AG92; -.
DR SMR; P0AG92; -.
DR STRING; 198214.SF0345; -.
DR EnsemblBacteria; AAN42003; AAN42003; SF0345.
DR EnsemblBacteria; AAP15880; AAP15880; S0353.
DR GeneID; 1027665; -.
DR GeneID; 66671293; -.
DR KEGG; sfl:SF0345; -.
DR KEGG; sfx:S0353; -.
DR PATRIC; fig|198214.7.peg.396; -.
DR HOGENOM; CLU_007894_4_3_6; -.
DR OMA; MVVYYRL; -.
DR OrthoDB; 121331at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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 Reference proteome; Translocation; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..615
FT /note="Protein translocase subunit SecD"
FT /id="PRO_0000095970"
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 548..570
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"
SQ SEQUENCE 615 AA; 66632 MW; 1099E6A9CC988EBE CRC64;
MLNRYPLWKY VMLIVVIVIG LLYALPNLFG EDPAVQITGA RGVAASEQTL IQVQKTLQEE
KITAKSVALE EGAILARFDS TDTQLRAREA LMGVMGDKYV VALNLAPATP RWLAAIHAEP
MKLGLDLRGG VHFLMEVDMD TALGKLQEQN IDSLRSDLRE KGIPYTTVRK ENNYGLSITF
RDAKARDEAI AYLSKRHPDL VISSQGSNQL RAVMSDARLS EAREYAVQQN INILRNRVNQ
LGVAEPVVQR QGADRIVVEL PGIQDTARAK EILGATATLE FRLVNTNVDQ AAAASGRVPG
DSEVKQTREG QPVVLYKRVI LTGDHITDST SSQDEYNQPQ VNISLDSAGG NIMSNFTKDN
IGKPMATLFV EYKDSGKKDA NGRAVLVKQE EVINIANIQS RLGNSFRITG INNPNEARQL
SLLLRAGALI APIQIVEERT IGPTLGMQNI EQGLEACLAG LLVSILFMII FYKKFGLIAT
SALIANLILI VGIMSLLPGA TLSMPGIAGI VLTLAVAVDA NVLINERIKE ELSNGRTVQQ
AIDEGYRGAF SSIFDANITT LIKVIILYAV GTGAIKGFAI TTGIGVATSM FTAIVGTRAI
VNLLYGGKRV KKLSI
