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Database: UniProt
Entry: V9XC15_9NOCA
LinkDB: V9XC15_9NOCA
Original site: V9XC15_9NOCA 
ID   V9XC15_9NOCA            Unreviewed;       598 AA.
AC   V9XC15;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-SEP-2017, entry version 22.
DE   RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   ORFNames=Y013_02120 {ECO:0000313|EMBL:AHD19579.1};
OS   Rhodococcus pyridinivorans SB3094.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1435356 {ECO:0000313|EMBL:AHD19579.1, ECO:0000313|Proteomes:UP000018781};
RN   [1] {ECO:0000313|EMBL:AHD19579.1, ECO:0000313|Proteomes:UP000018781}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB3094 {ECO:0000313|EMBL:AHD19579.1};
RX   PubMed=24874690;
RA   Dueholm M.S., Albertsen M., D'Imperio S., Tale V.P., Lewis D.,
RA   Nielsen P.H., Nielsen J.L.;
RT   "Complete Genome of Rhodococcus pyridinivorans SB3094, a Methyl-Ethyl-
RT   Ketone-Degrading Bacterium Used for Bioaugmentation.";
RL   Genome Announc. 2:e00525-14(2014).
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; CP006996; AHD19579.1; -; Genomic_DNA.
DR   RefSeq; WP_024100747.1; NC_023150.1.
DR   EnsemblBacteria; AHD19579; AHD19579; Y013_02120.
DR   GeneID; 29938645; -.
DR   KEGG; rpy:Y013_02120; -.
DR   PATRIC; fig|1435356.3.peg.415; -.
DR   KO; K03072; -.
DR   Proteomes; UP000018781; 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:UP000018781};
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:UP000018781};
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    408    428       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    435    457       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    463    484       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    512    531       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    537    563       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
SQ   SEQUENCE   598 AA;  61435 MW;  6FD47F3FEC8EB5AD CRC64;
     MAPSNGSVHP VRALALFGVI LAALYALVFF TGDKSPTPKL GIDLQGGTRV TLTARTPDGS
     SPSPDSLRQA QQIIETRVNG LGVSGSEVIV EGDNLVITVP GEDSAQARTL GQTARLYIRP
     VIGGPIDANM TAEDLAEQPG AGTPEGGLPA EPAPAEPAPG EPAPADQAPP ADAPEPQGRP
     FPAQDPTAPT DAPAPAETPE APVEAPQAPA EPSGAPEAPE NDGSLTPQEQ AAADIATAKA
     TRQSEDPAVQ QAAALALDCS AADPLAGNDD PALPLVACST DGTAIYLLGP SIIDGQQIED
     ATSGFNQQQS RYEVSLTFDS EGSNTWAQFT AANIGQQAAF VLDSKVVSAP VIQGATPAGS
     ATSITGQFTN TQAAELANTL KYGSLPLSFV ASEAETVSAT LGLASLEAGL IAGAVGLALV
     LLFCLAYYRM LGLLTALSLV LSGMAVYAVM VLLGRYIGFT LDLAGVAGLI IGIGMTADSF
     VVFFERIKDE IREGRSFRSA VPRGWARARR TILSGNAVSF IAAAVLYVLA VGQVRGFAFT
     LGLTTILDVV VVFLVTWPLV FLASKSKFWS KPSVNGLGAI QQVADERRLV AATAAKEA
//
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