ID A0A3R9UFG3_9ACTN Unreviewed; 604 AA.
AC A0A3R9UFG3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
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:RSS08852.1};
GN ORFNames=EF917_01260 {ECO:0000313|EMBL:RSS08852.1};
OS Streptomyces sp. WAC00469.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2487415 {ECO:0000313|EMBL:RSS08852.1, ECO:0000313|Proteomes:UP000269080};
RN [1] {ECO:0000313|EMBL:RSS08852.1, ECO:0000313|Proteomes:UP000269080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WAC00469 {ECO:0000313|EMBL:RSS08852.1,
RC ECO:0000313|Proteomes:UP000269080};
RA Culp E., Yim G., Waglechner N., Wang W., Pawlowski A.C., Wright G.D.;
RT "Unmasking the antibiotic production potential of Actinomycetes through
RT CRISPR/Cas9 inactivation of ubiquitous gene clusters.";
RL Submitted (NOV-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}.
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:RSS08852.1}.
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DR EMBL; RPRX01000002; RSS08852.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R9UFG3; -.
DR OrthoDB; 5240379at2; -.
DR Proteomes; UP000269080; 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; IPR004869; MMPL_dom.
DR InterPro; IPR005791; SecD.
DR InterPro; IPR022813; SecD/SecF_arch_bac.
DR InterPro; IPR022645; SecD/SecF_bac.
DR InterPro; IPR048631; SecD_1st.
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; PF03176; MMPL; 1.
DR Pfam; PF21760; SecD_1st; 1.
DR SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01463};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01463};
KW Protein transport {ECO:0000256|HAMAP-Rule:MF_01463};
KW Reference proteome {ECO:0000313|Proteomes:UP000269080};
KW Translocation {ECO:0000256|HAMAP-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}; Transport {ECO:0000256|HAMAP-Rule:MF_01463}.
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 429..453
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 459..480
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 508..527
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 533..552
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 73..130
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 395..567
FT /note="Membrane transport protein MMPL"
FT /evidence="ECO:0000259|Pfam:PF03176"
FT REGION 136..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 604 AA; 62502 MW; 638C81BEF5D303C6 CRC64;
MAAPKKGRSA GAQSKPWRSL VLILIAIVAL TGAMFASGHT APRLGIDLAG GTSITLRAVP
ERGQESAINK ANMDTAVSIM ERRVNGLGVS EAEVQTQGND NIIVNIPKGT NSQQAREQVG
TTAKLYFRPV LATDLSGAAA TPSPSSSASA DPSSSPSDEA GDDNGTSGGE KASSTDSATP
SATGSPQGRA VTDGLKADAT PSAGSTASGS PEASTGPSTD ATADSGSDGD IPAALQAQYA
TLDCTKQDVR ATAGKGVKPS EPTVACGENS QGQWQKYILG PAAVDGTDVK KAQAVFNTQT
AAGWTVTMEF TSKGAKKFAD ITGKLAQNPS PQNQFAIVLD GNVVSDPYVS QALTGGNAEI
TGRFSQEEAQ SLANMLSYGA LPLTFREDSV TTVTAALGSD QLRAGLIAGA IGLALVVVYL
LVFYRGLSII AIPSLLVSAI LTYTIMSLLG PAIGFALNLP AVCGAIVAIG ITADSFIVFF
ERIRDEIREG RSLRPAVERG WPRARRTILV SDFVSFLAAA VLFVVTVGKV QGFAFTLGLT
TLLDVVVVFL FTKPLMTILA RRKFFAQGHK WSGLDPKSLG AKPPLRRTRR PSSPAAGPVE
TKEA
//
