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Database: UniProt
Entry: A0A285NRC6_9AQUI
LinkDB: A0A285NRC6_9AQUI
Original site: A0A285NRC6_9AQUI 
ID   A0A285NRC6_9AQUI        Unreviewed;       497 AA.
AC   A0A285NRC6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   ORFNames=SAMN06265353_0414 {ECO:0000313|EMBL:SNZ12072.1};
OS   Hydrogenobacter hydrogenophilus.
OC   Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae;
OC   Hydrogenobacter.
OX   NCBI_TaxID=35835 {ECO:0000313|EMBL:SNZ12072.1, ECO:0000313|Proteomes:UP000218627};
RN   [1] {ECO:0000313|EMBL:SNZ12072.1, ECO:0000313|Proteomes:UP000218627}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2913 {ECO:0000313|EMBL:SNZ12072.1,
RC   ECO:0000313|Proteomes:UP000218627};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-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}.
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; OBEN01000001; SNZ12072.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285NRC6; -.
DR   OrthoDB; 9805019at2; -.
DR   Proteomes; UP000218627; 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; -; 2.
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        339..356
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        363..385
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        391..413
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        434..456
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        462..486
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   DOMAIN          133..190
FT                   /note="Protein translocase subunit SecDF P1"
FT                   /evidence="ECO:0000259|Pfam:PF21760"
FT   DOMAIN          319..487
FT                   /note="Protein export membrane protein SecD/SecF C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02355"
SQ   SEQUENCE   497 AA;  54723 MW;  A0C703F264B2514F CRC64;
     MRNFYFNLFT LLFLVVLSLT VSFFKPVNLG LDLKGGISML LEPDMDYALS QEYERYAKDI
     EEKVRTAGVN VLDIVVQKDG IKVETLDQKD AQKVFQIIQK DFPRFVVVST NKGEPLIRLK
     EEEINKLKES IVGQTVEVLR KRIDELGVVQ PVITKVGQDR VLVELPGVLD IEKAKSIIGR
     TALLELKLVV DSGSKEELEK KLTKDTELLP SKNPNEWFLV EKLPVITGAD LKTAYTSTDE
     FGAPAVTFEL TDRGAKLFGD ATEKNIGKRL AIVLDKKVMS APVIRSRISD RGQITGQFTP
     EEAKELAIVL RAGALPTAVK FLQETVVGPS LGRDAIQQSI KGGIVAFVLL VILLLARYKI
     AGITANLSII LNALLLWAGL VLIGATLTLP GIAGILLNMG IAVDSNVLIF ERVKEELRAG
     STFRKAVELG YRRSLSVVWD THITLLIAAL ILFQFGSGPV KGFATTLTIG SIASFISNVY
     FAKFFLDLLV KLKLLKI
//
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