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Database: UniProt
Entry: A0A1V0GVK7_9RHOB
LinkDB: A0A1V0GVK7_9RHOB
Original site: A0A1V0GVK7_9RHOB 
ID   A0A1V0GVK7_9RHOB        Unreviewed;       555 AA.
AC   A0A1V0GVK7;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
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:ARC37925.1};
GN   ORFNames=A6J80_17600 {ECO:0000313|EMBL:ARC37925.1}, H7K23_00660
GN   {ECO:0000313|EMBL:MBY0134576.1}, PY32053_01741
GN   {ECO:0000313|EMBL:AYF01368.1};
OS   Paracoccus yeei.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=147645 {ECO:0000313|EMBL:ARC37925.1, ECO:0000313|Proteomes:UP000191257};
RN   [1] {ECO:0000313|Proteomes:UP000191257}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FDAARGOS_252 {ECO:0000313|Proteomes:UP000191257};
RA   Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.,
RA   Sadzewicz L., Sengamalay N., Ott S., Godinez A., Nagaraj S., Nadendla S.,
RA   Geyer C., Sichtig H.;
RT   "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT   Supporting development and validation of Infectious Disease Dx tests.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ARC37925.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FDAARGOS_252 {ECO:0000313|EMBL:ARC37925.1};
RA   Campos J., Goldberg B., Tallon L., Sadzewicz L., Sengamalay N., Ott S.,
RA   Godinez A., Nagaraj S., Vyas G., Aluvathingal J., Nadendla S., Geyer C.,
RA   Nandy P., Hobson J., Sichtig H.;
RT   "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT   Supporting development and validation of Infectious Disease Dx tests.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AYF01368.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCUG 32053 {ECO:0000313|EMBL:AYF01368.1};
RX   PubMed=30410477; DOI=10.3389/fmicb.2018.02553;
RA   Lasek R., Szuplewska M., Mitura M., Decewicz P., Chmielowska C., Pawlot A.,
RA   Sentkowska D., Czarnecki J., Bartosik D.;
RT   "Genome Structure of the Opportunistic Pathogen Paracoccus yeei
RT   (Alphaproteobacteria) and Identification of Putative Virulence Factors.";
RL   Front. Microbiol. 9:2553-2553(2018).
RN   [4] {ECO:0000313|Proteomes:UP000272010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 32053 {ECO:0000313|Proteomes:UP000272010};
RA   Lasek R., Szuplewska M., Mitura M., Decewicz P., Chmielowska C., Pawlot A.,
RA   Sentkowska D., Czarnecki J., Bartosik D.;
RT   "Genome Structure of the Opportunistic Pathogen Paracoccus yeei
RT   (Alphaproteobacteria) and Identification of Putative Virulence Factors.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:MBY0134576.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S/N-202-OC-B2 {ECO:0000313|EMBL:MBY0134576.1};
RA   Seuylemezian A., Singh N.K., Wood J., Venkateswaran K.;
RT   "Fungal Genomes of the International Space Station.";
RL   Submitted (AUG-2020) 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}.
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DR   EMBL; CP020442; ARC37925.1; -; Genomic_DNA.
DR   EMBL; CP031078; AYF01368.1; -; Genomic_DNA.
DR   EMBL; JACLBQ010000001; MBY0134576.1; -; Genomic_DNA.
DR   STRING; 147645.A6J80_17600; -.
DR   KEGG; pye:A6J80_17600; -.
DR   eggNOG; COG0342; Bacteria.
DR   Proteomes; UP000191257; Chromosome.
DR   Proteomes; UP000272010; Chromosome.
DR   Proteomes; UP000756578; 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:UP000191257};
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        418..440
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        446..468
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        489..511
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        517..545
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   DOMAIN          187..244
FT                   /note="Protein translocase subunit SecDF P1"
FT                   /evidence="ECO:0000259|Pfam:PF21760"
FT   DOMAIN          374..545
FT                   /note="Protein export membrane protein SecD/SecF C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02355"
SQ   SEQUENCE   555 AA;  59372 MW;  3C52A5D442D2A250 CRC64;
     MLHIPTWKRL LILGLIAIGL LYAMPNLFYS RVEQHNDAIK TIERSGVETP EDVAARAGWP
     DWLPSGLVNL GLDLRGGAHL LGEVHVADVY KARMDALWPE LRDALVAQRD TVGAVRRIAS
     PDGGQLIVEI GNPDQMARAV EIARGLATPV TSLTGAGQSD IVATGSGNRL TVQLSDAEKA
     ATDDRTVQQS LEIIRRRIDE VGTREPTIMR QGKDRILIQV PGIGSAEELK QLIGTTAKLT
     FNPVVGRGTD PNARPGPGHV LLPSMDEPGV FYTLEENPVV TGEDLTDARP SFDQNGQPAV
     DFRFGPAGAK RFGAYTSANI GQPFAIVLDN QVISAPVIRQ AITTGSGQIS GAMDVDESTR
     LAVLLRAGAL PAEMTFLEER TIGPELGQDS IDAGRLSSII ATAAVVAYMI ASYGLFGVFA
     SIAVTVNVIL ILSIMSMMGA TLTLPGIAGI VLTVGTAVDA NVIIYERIRE ELRAGKRVVK
     AIDDGFNEAM SAIIDANVTS FISAAVMFFL GSGPVKGFAV TLTIGLVTSV FTAIYLTRLM
     IVFWLEWRKP KELIL
//
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