ID   A0A1P8XHJ0_9MYCO        Unreviewed;       595 AA.
AC   A0A1P8XHJ0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   03-MAY-2023, entry version 25.
DE   RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   ORFNames=BVC93_29165 {ECO:0000313|EMBL:AQA05768.1};
OS   Mycobacterium sp. MS1601.
OC   Bacteria; Actinomycetota; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1936029 {ECO:0000313|EMBL:AQA05768.1, ECO:0000313|Proteomes:UP000188050};
RN   [1] {ECO:0000313|EMBL:AQA05768.1, ECO:0000313|Proteomes:UP000188050}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS1601 {ECO:0000313|EMBL:AQA05768.1,
RC   ECO:0000313|Proteomes:UP000188050};
RX   PubMed=26804932; DOI=10.1016/j.jbiotec.2016.01.022;
RA   Sayed M., Dishisha T., Sayed W.F., Salem W.M., Temerk H.A., Pyo S.H.;
RT   "Selective oxidation of trimethylolpropane to 2,2-bis(hydroxymethyl)butyric
RT   acid using growing cells of Corynebacterium sp. ATCC 21245.";
RL   J. Biotechnol. 221:62-69(2016).
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; CP019420; AQA05768.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1P8XHJ0; -.
DR   STRING; 1936029.BVC93_29165; -.
DR   EnsemblBacteria; AQA05768; AQA05768; BVC93_29165.
DR   OrthoDB; 5240379at2; -.
DR   Proteomes; UP000188050; 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; 3.30.70.3220; -; 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; IPR022646; SecD/SecF_CS.
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; PF02355; SecD_SecF; 1.
DR   SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 1.
DR   TIGRFAMs; TIGR00916; 2A0604s01; 1.
DR   TIGRFAMs; TIGR01129; secD; 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        405..425
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        432..456
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        462..483
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        511..530
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        536..562
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   REGION          134..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..218
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   595 AA;  61725 MW;  C9AA9766DB0DCF96 CRC64;
     MASSTAPVHP YRYLTLFLVL LIGAFAAVFF TGDKQPEPKL GIDLQGGTRV TLTARTPDGS
     APTREALGQA QQIITSRVDG LGVSGSEVVI DGDNLVITVP GNDGNEARNL GQTARLYIRP
     VKYAVPVDQL AAATGQGQGQ PVPGGAPPVP GAPAPGQPPA GGVPGAPAAP PDAGLPAPEA
     PAAQPRPYPL EPAPTPPPTP GAPATPAAPA PAAPAPTGSQ APPDDRAALA ERIAFEKQLR
     QSDNESVQVL ALQYQAGRCN DDDVLAGNDD PNLPLVTCSE DKAVVYLLDP SIISGEQIAN
     ASSGFDQQQA RYIVDLEFKP EASDIWAQFT AQNIGTQTAF TLDSQVVSAP EIQEAIPGGR
     TQITGQFTQQ SAAELANVLK YGSLPLSFES SEAETVSATL GLQSLRAGLI AGAVGLAAVL
     LYSLLYYRVL GLLITVSLVA SGAMAYALLV LLGRYIGYTL DLAGIAGLII GIGTTADSFV
     VFFERIKDEI REGRSFRSAV PRGWARARKT IVSGNAVTFL AALVLYVLAV GQVKGFAFTL
     GLTTILDVLV VFLVTWPVIF LASKSTMLAK PAFNGLGAVQ QIARERRAAA SAGRG
//