ID A0A2S0WEE8_9CORY Unreviewed; 597 AA.
AC A0A2S0WEE8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN Name=secD {ECO:0000256|HAMAP-Rule:MF_01463,
GN ECO:0000313|EMBL:AWB84120.1};
GN ORFNames=C3E79_06195 {ECO:0000313|EMBL:AWB84120.1}, DF219_02835
GN {ECO:0000313|EMBL:PWC00131.1};
OS Corynebacterium liangguodongii.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=2079535 {ECO:0000313|EMBL:AWB84120.1, ECO:0000313|Proteomes:UP000244754};
RN [1] {ECO:0000313|EMBL:AWB84120.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2184 {ECO:0000313|EMBL:AWB84120.1};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PWC00131.1, ECO:0000313|Proteomes:UP000245180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2185 {ECO:0000313|EMBL:PWC00131.1,
RC ECO:0000313|Proteomes:UP000245180};
RA Liu S., Wang Z., Li J.;
RL Submitted (APR-2018) 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. Other proteins may also be involved.
CC {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}.
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DR EMBL; CP026948; AWB84120.1; -; Genomic_DNA.
DR EMBL; QEEY01000002; PWC00131.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S0WEE8; -.
DR KEGG; clia:C3E79_06195; -.
DR OrthoDB; 5240379at2; -.
DR Proteomes; UP000244754; Chromosome.
DR Proteomes; UP000245180; 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; 3.30.70.3220; -; 1.
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; IPR022813; SecD/SecF_arch_bac.
DR InterPro; IPR022645; SecD/SecF_bac.
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; 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 21..40
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 430..452
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 458..479
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 507..526
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 532..557
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 390..557
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 597 AA; 62372 MW; 97564F59FEA906FA CRC64;
MSAHTRRTAQ ARAKRAWPAR ALALFLLAIV AVYALVFFTG NRAAIPKLGI DLQGGTRVTL
VPQGEEPTRE QLEDARNIIE SRVNGMGVTG ASVVVDGNTL VITAAGDDTS SVREIGQTSQ
LAFRPVASSP MPDPAAVGEA LKNTADRWVE YSVIPAEQAQ STLDEIAKQL GDAAGELKVS
TAPLSEPQGP VEAKERRQAT TEMLRETRQS DDPTQQFASL ALMSLACGAQ ESDPLAGSDD
LAATLVACDS TTKQPLLLGA APLLDENGDQ AGPRLTGNEI DTARPITGGY NPQSGQMEIS
FAFSQAGDVN GSQAWAGLTS QMIGQQVAIT LDSQVISAPV IQGATPVGSA TSITGQFTQE
EATALANNLR YGALPLSFAG EDGEPGGTAT TVPPSLGAAS LKAGLIAGLV GLGLVAVFVF
AYYRLFGLIS LATLAVAGLV VYGVLVLLGR WIGYSLDLSG VAGLIIGIGT TADSFVVIYE
RIKDELRKGR TFRSATAQGW DRAKETIVTG NIVTLIGAVV IYFLAVGDVK GFAFTMGLTT
VVDLLVTFTV TAPLMILASR TRFFSRGGVN GMGKIFRLVE AERAQATTGT TTANEEM
//
