ID A0A5C4VVD0_9ACTN Unreviewed; 616 AA.
AC A0A5C4VVD0;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 24-JAN-2024, entry version 13.
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:TNM39496.1};
GN ORFNames=FHP29_11415 {ECO:0000313|EMBL:TNM39496.1};
OS Nocardioides albidus.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1517589 {ECO:0000313|EMBL:TNM39496.1, ECO:0000313|Proteomes:UP000313231};
RN [1] {ECO:0000313|EMBL:TNM39496.1, ECO:0000313|Proteomes:UP000313231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCTCC AB 2015297 {ECO:0000313|EMBL:TNM39496.1,
RC ECO:0000313|Proteomes:UP000313231};
RX PubMed=26530636; DOI=.1099/ijsem.0.000730;
RA Singh H., Du J., Trinh H., Won K., Yang J.E., Yin C., Kook M., Yi T.H.;
RT "Nocardioides albidus sp. nov., an actinobacterium isolated from garden
RT soil.";
RL Int. J. Syst. Evol. Microbiol. 66:371-378(2016).
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:TNM39496.1}.
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DR EMBL; VDMP01000024; TNM39496.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5C4VVD0; -.
DR OrthoDB; 5240379at2; -.
DR Proteomes; UP000313231; 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}; Reference proteome {ECO:0000313|Proteomes:UP000313231};
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 420..440
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 447..467
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 479..498
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 527..544
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 550..569
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 68..126
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 402..577
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
FT REGION 136..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 616 AA; 64742 MW; 181B059FF8FB1134 CRC64;
MASRRPRPGR NLIAFFLGLA ILYGLTALSQ ASVDEPETPW RPALGLDLQG GTRITLTAEK
APTKENLDEA RRIIDQRVNG SGVAEAAVTT QGGRNIVVEV PGKTKDRDRL EQTVKRQAQL
RFRLVACSDI RPAACDTSGA GTGGLGGGLG RAPLSLAEDD PTDGATDKPS GGATDQPADG
ATASTDAPTG VPTDVPTDVP TDGATPGTTP TAEDPGADGK KWTVKDDIAW SRSPDQEAIT
AYNTYSCDEK GVLVDAEGKP ADLPDDPDKS LVACSKPEKD TGVIKFLLSR SVVEGTELDD
ASAQTPQNGV GWVVAIEMGN SKDRAHPKGS TGAAADFEAV TRAFAGTDEQ FAVVLDAQVL
TYPVLNSVIT DGRSQIEGDF SEQEALDLAN SLKFGALPIK FNDKQTSVEE IGPSLAGNQL
SAGLTAGAIG LVLVMLYCLF YYRGLGLVVV TSLFVAAAVT YAMVLLLSKT AGFTLTLPGI
AGLVIAVGIT ADSFVIFFER IRDEMREGKS MRVAVETGWA RARVTRVAAN TVQILSALVL
YIFATGAVKG FGFALGLTTL IDLAVLFWFT KPMVSWLAQF KVFNSGHKLS GLSKETLGMD
VTPSRPRRTA VAGGDA
//
