ID A0A239FPQ5_9ACTN Unreviewed; 602 AA.
AC A0A239FPQ5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-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=SAMN06265355_12181 {ECO:0000313|EMBL:SNS58819.1};
OS Actinomadura mexicana.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinomadura.
OX NCBI_TaxID=134959 {ECO:0000313|EMBL:SNS58819.1, ECO:0000313|Proteomes:UP000198420};
RN [1] {ECO:0000313|EMBL:SNS58819.1, ECO:0000313|Proteomes:UP000198420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44485 {ECO:0000313|EMBL:SNS58819.1,
RC ECO:0000313|Proteomes:UP000198420};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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; FZNP01000021; SNS58819.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239FPQ5; -.
DR Proteomes; UP000198420; 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; 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; 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 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 434..455
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 467..488
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 509..530
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 536..556
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 65..121
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 389..565
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
FT REGION 127..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 602 AA; 62012 MW; C4F560260079ADA4 CRC64;
MAPPKNAPKP GRTLLALFAI MVVMAGLAVW QGQTKPKLGL DLAGGTTVTL TAKTANGKNP
PANQMNQAVK IMTKRVNGLG VSDAEVAKQG SNNIVVNVPG EGQGRVVNLI GTTAKLQFRQ
VFAVADGKPS SGAVPAPSPS PSKGTGEKKD GGKSPSPSAS ASPSGGASPS ASSTPRGRAL
SGALTAPTPK PSGSAAPSSA PSASSPLGQP SGQPTAPTQD YPGVTDKAVI SQFEALNCYT
GDRRAPGSND PNRKFVASCD QDEESGQAAK YILGPVRVLG ENVSSASAMP PNAQNGQASW
SVSLKFDGTG ARQFGEVTTA ASQAYQQNPS SPQAQVAIVL DGQVVSAPSI REGAITGGTA
SIDGPPDSFN QQYATDLANV LKYGALPLEF KQSSIDEVSS TLGSDQLTGG LIAGAIGLGL
VLLYCLFYYR GLGLVAVSSL VVASVITYEA VVILGEGMGF RLSLPHIIGL IVSIGITADS
FIVYFERLRD ELRAGRKLRS SVENAWKRAR RTILVADAVT FLAALVLYFL AVGGVAGFAF
AMGLTTLIDV VVVFFFTKPL VALLARTSFF GRGHPMSGLD PRRLHKAQDT SAPAARTTSQ
EA
//
