SECD_ECO57
ID SECD_ECO57 Reviewed; 615 AA.
AC P0AG91; P19673; P72348; P77531;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Protein translocase subunit SecD {ECO:0000255|HAMAP-Rule:MF_01463};
GN Name=secD {ECO:0000255|HAMAP-Rule:MF_01463};
GN OrderedLocusNames=Z0507, ECs0459;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG54755.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB33882.1; -; Genomic_DNA.
DR PIR; C90686; C90686.
DR PIR; G85536; G85536.
DR RefSeq; NP_308486.1; NC_002695.1.
DR RefSeq; WP_000934822.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AG91; -.
DR SMR; P0AG91; -.
DR STRING; 155864.EDL933_0473; -.
DR PRIDE; P0AG91; -.
DR EnsemblBacteria; AAG54755; AAG54755; Z0507.
DR EnsemblBacteria; BAB33882; BAB33882; ECs_0459.
DR GeneID; 66671293; -.
DR GeneID; 914561; -.
DR KEGG; ece:Z0507; -.
DR KEGG; ecs:ECs_0459; -.
DR PATRIC; fig|386585.9.peg.559; -.
DR eggNOG; COG0342; Bacteria.
DR HOGENOM; CLU_007894_4_3_6; -.
DR OMA; MVVYYRL; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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_0000095961"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..29
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TOPO_DOM 30..455
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 456..472
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TOPO_DOM 473..476
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TOPO_DOM 498..501
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 502..518
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TOPO_DOM 519..563
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 564..580
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TOPO_DOM 581..585
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 586..605
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TOPO_DOM 606..615
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
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
