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Database: UniProt
Entry: A0A4Z1CQI9_9RHOB
LinkDB: A0A4Z1CQI9_9RHOB
Original site: A0A4Z1CQI9_9RHOB 
ID   A0A4Z1CQI9_9RHOB        Unreviewed;       554 AA.
AC   A0A4Z1CQI9;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-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:TGN67322.1};
GN   ORFNames=E4L95_05305 {ECO:0000313|EMBL:TGN67322.1};
OS   Paracoccus liaowanqingii.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=2560053 {ECO:0000313|EMBL:TGN67322.1, ECO:0000313|Proteomes:UP000297972};
RN   [1] {ECO:0000313|EMBL:TGN67322.1, ECO:0000313|Proteomes:UP000297972}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3058 {ECO:0000313|EMBL:TGN67322.1,
RC   ECO:0000313|Proteomes:UP000297972};
RA   Li J.;
RL   Submitted (MAR-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-YajC and YidC. {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:TGN67322.1}.
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DR   EMBL; SRPG01000033; TGN67322.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4Z1CQI9; -.
DR   Proteomes; UP000297972; 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; 3.30.70.3400; -; 1.
DR   Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 1.
DR   HAMAP; MF_01463_B; SecD_B; 1.
DR   InterPro; IPR001036; Acrflvin-R.
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   PRINTS; PR00702; ACRIFLAVINRP.
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        417..439
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        445..467
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        488..510
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        516..544
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   DOMAIN          186..243
FT                   /note="Protein translocase subunit SecDF P1"
FT                   /evidence="ECO:0000259|Pfam:PF21760"
FT   DOMAIN          373..544
FT                   /note="Protein export membrane protein SecD/SecF C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02355"
SQ   SEQUENCE   554 AA;  59182 MW;  8162687567D96B9B CRC64;
     MLQIDRWKRV LIFGICLLGL FYALPNAFYA RVEAHNDAVA RIEATGVETP ELVAARDGWP
     SWMPSNLVNL GLDLRGGAHL LGEVQVTQVY KTRVDALWPE LRTALAAERD TVGAIRRVEA
     PEGVLSVEIG NADQMPRAIE IARGFSDPVT TLTGAGQQSL AIATQGATLT IQLSDAEKAV
     TDDRTIQQSL EIVRRRVDEV GTREPTIMRQ GEDRILIQVP GIGSATELKE LIGTTAQLTF
     NPVLGTTGDA EAQPGLGQFI APSIDQEGVY YILEDSPVVT GEDLVDAMPG SDENGQPSVN
     FRFNPTGARA FGSYTSQNIG QPFAIVLDDE VISAPVIRSA ITTGSGQISG SMNFDQANQL
     SVLLRAGALP AEMTFLEERT VGPELGQDSV DAGKVAAGVG FVAVVMLMIL SYGRFGVFAA
     VALTFNMVLL FAVLSLIGAT LTLPGIAGIV LTIGMAVDAN VLVFERIREE LRTARGPARA
     IELGYEKAMS AIVDANITTL IVAAILFVLG SGPVKGFAVT LTIGIVTSVF TALFVTRLIT
     IMWFERARPK QIEV
//
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