ID   SECD_VIBAL              Reviewed;         618 AA.
AC   E9RGS3;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   25-MAY-2022, entry version 38.
DE   RecName: Full=Protein translocase subunit SecD;
GN   Name=secD;
OS   Vibrio alginolyticus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=138-2;
RA   Tsukazaki T., Mori H., Echizen Y., Ishitani R., Fukai S., Tanaka T.,
RA   Sasaki Y., Mio K., Kuwata M., Perederina A., Vassylyev D.G., Kohno T.,
RA   Sato C., Maturana A., Ito K., Nureki O.;
RT   "Structure and function of SecDF, a protein export-enhancing membrane
RT   component.";
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION IN E.COLI, FUNCTION IN PROTEIN TRANSLOCATION, AND MUTAGENESIS OF
RP   ASP-206 AND ARG-240.
RC   STRAIN=138-2;
RX   PubMed=21562494; DOI=10.1038/nature09980;
RA   Tsukazaki T., Mori H., Echizen Y., Ishitani R., Fukai S., Tanaka T.,
RA   Perederina A., Vassylyev D.G., Kohno T., Maturana A.D., Ito K., Nureki O.;
RT   "Structure and function of a membrane component SecDF that enhances protein
RT   export.";
RL   Nature 474:235-238(2011).
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 (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: Expression of V.alginolyticus SecDF in an E.coli secDF mutant
CC       restores protein export in a Na(+)-dependent manner, strongly
CC       suggesting SecDF functions via cation-coupled protein translocation.
CC       {ECO:0000269|PubMed:21562494}.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SecD/SecF family. SecD subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AB583186; BAJ78589.1; -; Genomic_DNA.
DR   RefSeq; WP_006741889.1; NZ_PZOD01000080.1.
DR   AlphaFoldDB; E9RGS3; -.
DR   SMR; E9RGS3; -.
DR   STRING; 663.BAU10_01930; -.
DR   eggNOG; COG0342; Bacteria.
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; IPR001036; Acrflvin-R.
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   PANTHER; PTHR30081; PTHR30081; 1.
DR   Pfam; PF07549; Sec_GG; 1.
DR   Pfam; PF13721; SecD-TM1; 1.
DR   Pfam; PF02355; SecD_SecF; 1.
DR   PRINTS; PR00702; ACRIFLAVINRP.
DR   TIGRFAMs; TIGR00916; 2A0604s01; 1.
DR   TIGRFAMs; TIGR01129; secD; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Membrane; Protein transport; Translocation; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..618
FT                   /note="Protein translocase subunit SecD"
FT                   /id="PRO_0000412685"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        455..475
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        477..497
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        508..528
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        563..583
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        587..607
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         206
FT                   /note="D->N: Nearly abolishes protein translocation."
FT                   /evidence="ECO:0000269|PubMed:21562494"
FT   MUTAGEN         240
FT                   /note="R->M: Nearly abolishes protein translocation."
FT                   /evidence="ECO:0000269|PubMed:21562494"
SQ   SEQUENCE   618 AA;  66919 MW;  A2441A9AB9C2B382 CRC64;
     MLNRYPLWKY LMVFFAIITA ALYALPNIYG EDPAIQVTGA RGASVDMSTL DAVTTALDKE
     QLSHKSIALE NGSILVRFND TDTQISARDV ISEALGKDTI VALNLAPSTP DWLEAIGASP
     LKLGLDLRGG VHFLMEVDMD AAMEKLVGQQ EEAFRSELRE AKIRYRAIRP SGKEAVEVLL
     RNEEQLAEAK AMLEKNHPDM LFVESDSNGR YALTATFTEQ RLQEIRNYAV EQNITILRNR
     VNELGVAEPL VQRQGASRIV VELPGVQDTA RAKEILGATA TLEFREVDDK ADLSAAANGR
     APAGSEIKMD RDGRPVVLKK RVILGGQSIT DASSSVDEYG RPQVNISLDS EGGNKMSAFS
     KKNIGKLMAT VFAEYKDSGR RTPEGKVILD KHEEVINQAT IQSALGRNFR ITGIDSAAEA
     HNLALLLRAG ALIAPISIVE ERTIGPSMGQ QNIDMGIQAC IWGMVAVMLF TLLYYRGFGL
     IANIALMANL VLIIGVMSMI PGATMTLPGI AGIVLTVGMA VDANVLIFER IREELRDGRS
     PQQAIHQGYA NAFSTIADAN ITTLITAIIL FAVGTGAVKG FAVTLSIGIL TSMFTAIIGT
     RCIVNLIYGG KRVDKLSI