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Database: UniProt
Entry: G8RIN2_MYCRN
LinkDB: G8RIN2_MYCRN
Original site: G8RIN2_MYCRN 
ID   G8RIN2_MYCRN            Unreviewed;       595 AA.
AC   G8RIN2;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   28-MAR-2018, entry version 38.
DE   RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   OrderedLocusNames=MycrhN_5466 {ECO:0000313|EMBL:AEV75939.1};
OS   Mycobacterium rhodesiae (strain NBB3).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=710685 {ECO:0000313|EMBL:AEV75939.1, ECO:0000313|Proteomes:UP000005442};
RN   [1] {ECO:0000313|EMBL:AEV75939.1, ECO:0000313|Proteomes:UP000005442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBB3 {ECO:0000313|EMBL:AEV75939.1,
RC   ECO:0000313|Proteomes:UP000005442};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Gu W., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Mattes T.,
RA   Holmes A., Rutledge P., Paulsen I., Coleman N., Woyke T.;
RT   "Complete sequence of Mycobacterium rhodesiae NBB3.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Part of the Sec protein translocase complex. Interacts
CC       with the SecYEG preprotein conducting channel. SecDF uses the
CC       proton motive force (PMF) to complete protein translocation after
CC       the ATP-dependent function of SecA. {ECO:0000256|HAMAP-
CC       Rule:MF_01463, ECO:0000256|SAAS:SAAS00541769}.
CC   -!- SUBUNIT: Forms a complex with SecF. Part of the essential Sec
CC       protein translocation apparatus which comprises SecA, SecYEG and
CC       auxiliary proteins SecDF. Other proteins may also be involved.
CC       {ECO:0000256|HAMAP-Rule:MF_01463}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01463}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01463}.
CC   -!- SIMILARITY: Belongs to the SecD/SecF family. SecD subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01463}.
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DR   EMBL; CP003169; AEV75939.1; -; Genomic_DNA.
DR   RefSeq; WP_014213678.1; NC_016604.1.
DR   STRING; 710685.MycrhN_5466; -.
DR   EnsemblBacteria; AEV75939; AEV75939; MycrhN_5466.
DR   KEGG; mrh:MycrhN_5466; -.
DR   PATRIC; fig|710685.3.peg.5490; -.
DR   eggNOG; ENOG4107RSV; Bacteria.
DR   eggNOG; COG0342; LUCA.
DR   KO; K03072; -.
DR   OMA; ADSFVVY; -.
DR   OrthoDB; POG091H02C5; -.
DR   BioCyc; MRHO710685:G1H0U-5391-MONOMER; -.
DR   Proteomes; UP000005442; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005622; C:intracellular; IEA:GOC.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015450; F:P-P-bond-hydrolysis-driven protein transmembrane transporter 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   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   Pfam; PF07549; Sec_GG; 1.
DR   Pfam; PF02355; SecD_SecF; 1.
DR   TIGRFAMs; TIGR00916; 2A0604s01; 1.
DR   TIGRFAMs; TIGR01129; secD; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00425060};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005442};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00284057};
KW   Protein transport {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00425133};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005442};
KW   Translocation {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00425069};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00425065};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00425143};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00425109}.
FT   TRANSMEM     12     30       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    404    424       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    431    455       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    461    482       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    510    529       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    535    561       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
SQ   SEQUENCE   595 AA;  62484 MW;  D5C8A227A08DBC60 CRC64;
     MASSSTPVHP ARYLAFFLVL LVGAYLLVFL TGDKKAEPKL GIDLQGGTRV TLTARTPDGS
     RPTRDALNQA QTIISDRVNG LGVSGSEVII DGDNLVITVP GNESSEARNL GQTARLYIRP
     VIHAMPAAGQ GQQPPTEAPQ GAPPGAPGAI PGVPGAEPGA PAPGGAGTPP AAPPQTPAPQ
     PRPYPEQPPT QPTPSPSPSQ PAPPPGTAQQ PPPPGQQPPP PNPNDIPLSQ RIADEKELRQ
     SADQQIQILA LQFQATRCGQ DDVLAGNDDP NLPLVTCSQN GQEVYLLDKS IISGEQIENA
     SSGLDQQQGQ YIVDLQFKSD ATKIWSDFTA ANVGTQTAFV LDSQVVSAPE IREPIPGGRT
     QISGQFTEQT ARELANVLKY GSLPLSFESS EAETVSATLG LTSLRAGLIA GAVGLALVLL
     YSLLYYRILG VLIGLSLVAS GAMVYAILVL LGRYIGYTLD LAGIAGLIIG IGMTADSFVV
     FFERIKDEIR DGRSFRSAVP RGWNRARKTI LSGNAVTFLA AAVLYVLAVG QVKGFAFTLG
     LTTILDVVVV FLVTWPIVYI ASKSPTMAKP RLNGLGAVQQ IARERRAAAH VTGRG
//
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