ID A0A1X3L7J5_ECOLX Unreviewed; 615 AA. AC A0A1X3L7J5; DT 05-JUL-2017, integrated into UniProtKB/TrEMBL. DT 05-JUL-2017, sequence version 1. DT 24-JAN-2024, entry version 18. DE RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463}; GN Name=secD {ECO:0000256|HAMAP-Rule:MF_01463}; GN ORFNames=EAVG_02252 {ECO:0000313|EMBL:OSL66086.1}; OS Escherichia coli H420. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=656400 {ECO:0000313|EMBL:OSL66086.1, ECO:0000313|Proteomes:UP000193619}; RN [1] {ECO:0000313|EMBL:OSL66086.1, ECO:0000313|Proteomes:UP000193619} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H420 {ECO:0000313|EMBL:OSL66086.1, RC ECO:0000313|Proteomes:UP000193619}; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Richards J., Roberts A., Saif S., RA Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., RA Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia coli H420."; RL Submitted (APR-2010) 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:0000256|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: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: 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:OSL66086.1}. 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; ADJZ01000013; OSL66086.1; -; Genomic_DNA. DR RefSeq; WP_000934822.1; NZ_ADJZ01000013.1. DR AlphaFoldDB; A0A1X3L7J5; -. DR SMR; A0A1X3L7J5; -. DR GeneID; 75202830; -. DR Proteomes; UP000193619; Unassembled WGS sequence. 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 Gene3D; 3.30.1360.200; -; 1. DR Gene3D; 3.30.70.260; -; 1. DR Gene3D; 3.30.70.3400; -; 2. DR Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 1. 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 InterPro; IPR048631; SecD_1st. DR InterPro; IPR048634; SecD_SecF_C. DR NCBIfam; TIGR00916; 2A0604s01; 1. DR NCBIfam; TIGR01129; secD; 1. DR PANTHER; PTHR30081:SF1; PROTEIN TRANSLOCASE SUBUNIT SECD; 1. DR PANTHER; PTHR30081; PROTEIN-EXPORT MEMBRANE PROTEIN SEC; 1. DR Pfam; PF07549; Sec_GG; 1. DR Pfam; PF13721; SecD-TM1; 1. DR Pfam; PF21760; SecD_1st; 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}; 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 7..25 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463" FT TRANSMEM 453..472 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463" FT TRANSMEM 477..497 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463" FT TRANSMEM 503..524 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463" FT TRANSMEM 545..571 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463" FT TRANSMEM 577..605 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463" FT DOMAIN 2..103 FT /note="SecD export protein N-terminal TM" FT /evidence="ECO:0000259|Pfam:PF13721" FT DOMAIN 227..285 FT /note="Protein translocase subunit SecDF P1" FT /evidence="ECO:0000259|Pfam:PF21760" FT DOMAIN 433..601 FT /note="Protein export membrane protein SecD/SecF C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF02355" 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 //