ID A0A5S4G5H5_9ACTN Unreviewed; 592 AA.
AC A0A5S4G5H5;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 24-JAN-2024, entry version 12.
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:TMR28255.1};
GN ORFNames=ETD85_36495 {ECO:0000313|EMBL:TMR28255.1};
OS Nonomuraea zeae.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=1642303 {ECO:0000313|EMBL:TMR28255.1, ECO:0000313|Proteomes:UP000306628};
RN [1] {ECO:0000313|EMBL:TMR28255.1, ECO:0000313|Proteomes:UP000306628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100528 {ECO:0000313|EMBL:TMR28255.1,
RC ECO:0000313|Proteomes:UP000306628};
RA Saricaoglu S., Isik K.;
RT "Draft genome sequence of Nonomuraea zeae DSM 100528.";
RL Submitted (MAY-2019) 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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:TMR28255.1}.
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DR EMBL; VCKX01000147; TMR28255.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5S4G5H5; -.
DR OrthoDB; 5240379at2; -.
DR Proteomes; UP000306628; 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; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000306628};
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 401..419
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 426..447
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 459..477
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 511..534
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 540..558
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 51..105
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 381..557
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
FT REGION 117..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 592 AA; 61630 MW; 32CFDF5492F896D4 CRC64;
MLLALILALG GTMFLQKAFT PKLGLDLAGG TTVTLSPVTQ NNAAPPEEIL DRAVNIIRDR
VNGTGISDAE VAKSGDNIII SIPGVGQSEA VKLVATTAEL RFRQVLAMAA TQVPQDLATN
APTPSASTSG APSAKPSASQ PAGTPKPSTS ASAPQPSTSP TGKALSSALT QATPAPSPTA
TQSGQKQQET SGQKQQETKK GQDAKSSPTA SPSAQASTPP AEDPTAGINT QGIDPAVLAQ
FNKLDCADPA NRGQGVQDDP NKQYAGCETD GSYKYVLDVA KVVGTDIDTA SAGIRQGTTE
WIVQLDFKSK GAAEWSTLTT AAYNSQEPRN KVAVVLDGVV ITAPNIISPI PGGRAEITGG
FDQISATNLA DQLKYGALPL KFNRSSIDTV SSTLGQDQLE GGLVAGLIGL ALVVVYCLLY
YRGLGIVAVL SLVIATIITY TAVVVLGHNA GFRLSLPHII GLVVSIGITA DSFIVYFERI
RDEMKEGRRS LRAAVEVAWV RARRTILIAD AVMFIAAIVL YFLAVGGVAG FAFAMGLTTL
IDIVVVFLFT KPFIALLARV KFFAKGHPLS GLDAERMSEV GTTGRTTTPQ EA
//
