ID I0HLA8_RUBGI Unreviewed; 635 AA.
AC I0HLA8;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
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:BAL93795.1};
GN OrderedLocusNames=RGE_04500 {ECO:0000313|EMBL:BAL93795.1};
OS Rubrivivax gelatinosus (strain NBRC 100245 / IL144).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Rubrivivax.
OX NCBI_TaxID=983917 {ECO:0000313|EMBL:BAL93795.1, ECO:0000313|Proteomes:UP000007883};
RN [1] {ECO:0000313|EMBL:BAL93795.1, ECO:0000313|Proteomes:UP000007883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100245 / IL144 {ECO:0000313|Proteomes:UP000007883};
RX PubMed=22689232; DOI=10.1128/JB.00511-12;
RA Nagashima S., Kamimura A., Shimizu T., Nakamura-isaki S., Aono E.,
RA Sakamoto K., Ichikawa N., Nakazawa H., Sekine M., Yamazaki S., Fujita N.,
RA Shimada K., Hanada S., Nagashima K.V.P.;
RT "Complete genome sequence of phototrophic betaproteobacterium Rubrivivax
RT gelatinosus IL144.";
RL J. Bacteriol. 194:3541-3542(2012).
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 inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_01463}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01463}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC membrane protein {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; AP012320; BAL93795.1; -; Genomic_DNA.
DR RefSeq; WP_014426671.1; NC_017075.1.
DR AlphaFoldDB; I0HLA8; -.
DR STRING; 983917.RGE_04500; -.
DR KEGG; rge:RGE_04500; -.
DR PATRIC; fig|983917.3.peg.442; -.
DR eggNOG; COG0342; Bacteria.
DR HOGENOM; CLU_007894_4_3_4; -.
DR Proteomes; UP000007883; Chromosome.
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; IPR027398; SecD-TM.
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; PF13721; SecD-TM1; 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 inner membrane {ECO:0000256|HAMAP-Rule:MF_01463};
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:UP000007883};
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 455..472
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 574..598
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 1..98
FT /note="SecD export protein N-terminal TM"
FT /evidence="ECO:0000259|Pfam:PF13721"
FT DOMAIN 236..295
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 430..601
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 635 AA; 68773 MW; C6F77CB8A10EC1E8 CRC64;
MNRYPWWKYA ILAFAFVVGL LYTVPNFYGE APAVQVSSGK ATVKMDPAMV QRVEQILSSA
GLKADFVQLD GTSVRARFDD TDTQIKAKDA IAHALNPDAN DPTWIVALNL VSRSPQWMAR
IHALPMYLGL DLRGGVHFLM QVDMKAALTK KAEAVAGDVR TLLRDKNIRH AGITREGNAV
EVRFRETALA EQARSLLTDQ LPDLQWTPTA DAATGDTKLV GTLKPQAATR VQEQALKQNI
STLNNRVNEL GVAEPVIQQQ GIDRVVVQLP GVQDTAKAKD IIGRTATLEI RLVNETNEAM
DAVRGSGPVP FGSERFLERG GQPVIVYRNV VLTGENLTDA QPGFDGQTHE PTVNLTLDAR
GARIFKDVTR ENVGKRMAIL LFEKGKGEVV TAPVIRSEIG GGRVQISGRM TTEEASDQAL
LLRAGSLAAP MEIIEERTIG PSLGAENIAK GFHSVLWGFV AIAIFMCLYY MLFGVFSTLA
LAFNLLMLIA VLSMLQATLS LPGIAAIALV LGMAIDSNVL INERVREELR HGATPQVAIN
AGYERAFGTI LDSNVTTLIA GLALLAFGSG PVRGFAVVHC LGILTSMFSS VMFSRGLVNL
WYGRQKKLKS VSIGQVWRPD GGTPVPAEDK QNAKA
//
