ID   SECD_MYCTO              Reviewed;         573 AA.
AC   P9WGP0; L0TCU8; Q50634;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=Protein translocase subunit SecD {ECO:0000255|HAMAP-Rule:MF_01463};
GN   Name=secD {ECO:0000255|HAMAP-Rule:MF_01463}; OrderedLocusNames=MT2664;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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:0000255|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:0000255|HAMAP-Rule:MF_01463}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01463};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01463}.
CC   -!- SIMILARITY: Belongs to the SecD/SecF family. SecD subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01463}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK46977.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK46977.1; ALT_INIT; Genomic_DNA.
DR   PIR; B70726; B70726.
DR   RefSeq; WP_003413385.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WGP0; -.
DR   SMR; P9WGP0; -.
DR   EnsemblBacteria; AAK46977; AAK46977; MT2664.
DR   GeneID; 45426589; -.
DR   KEGG; mtc:MT2664; -.
DR   PATRIC; fig|83331.31.peg.2871; -.
DR   HOGENOM; CLU_007894_4_2_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   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; PTHR30081; 1.
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; Membrane; Protein transport; Translocation; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..573
FT                   /note="Protein translocase subunit SecD"
FT                   /id="PRO_0000428328"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT   TRANSMEM        385..405
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT   TRANSMEM        410..430
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT   TRANSMEM        441..461
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT   TRANSMEM        489..509
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT   TRANSMEM        514..534
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT   REGION          127..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..196
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   573 AA;  60267 MW;  5A8F42E2C0389CE2 CRC64;
     MASSSAPVHP ARYLSVFLVM LIGIYLLVFF TGDKHTAPKL GIDLQGGTRV TLTARTPDGS
     APSREALAQA QQIISARVNG LGVSGSEVVV DGDNLVITVP GNDGSEARNL GQTARLYIRP
     VLNSMPAQPA AEEPQPAPSA EPQPPGQPAA PPPAQSGAPA SPQPGAQPRP YPQDPAPSPN
     PTSPASPPPA PPAEAPATDP RKDLAERIAQ EKKLRQSTNQ YMQMVALQFQ ATRCESDDIL
     AGNDDPKLPL VTCSTDHKTA YLLAPSIISG DQIQNATSGM DQRGIGYVVD LQFKGPAANI
     WADYTAAHIG TQTAFTLDSQ VVSAPQIQEA IPGGRTQISG GDPPFTAATA RQLANVLKYG
     SLPLSFEPSE AQTVSATLGL SSLRAGMIAG AIGLLLVLVY SLLYYRVLGL LTALSLVASG
     SMVFAILVLL GRYINYTLDL AGIAGLIIGI GTTADSFVVF FERIKDEIRE GRSFRSAVPR
     GWARARKTIV SGNAVTFLAA AVLYFLAIGQ VKGFAFTLGL TTILDLVVVF LVTWPLVYLA
     SKSSLLAKPA YNGLGAVQQV ARERRAMART GRG