ID   SECD_PROMA              Reviewed;         494 AA.
AC   Q7VCH3;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Protein translocase subunit SecD {ECO:0000255|HAMAP-Rule:MF_01463};
GN   Name=secD {ECO:0000255|HAMAP-Rule:MF_01463}; OrderedLocusNames=Pro_0767;
OS   Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167539;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARG / CCMP1375 / SS120;
RX   PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA   Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA   Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA   Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA   Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT   "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT   nearly minimal oxyphototrophic genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
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   -!- FUNCTION: Probably participates in protein translocation into and
CC       across both the cytoplasmic and thylakoid membranes in cyanobacterial
CC       cells. {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 inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01463}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01463}.
CC   -!- SIMILARITY: Belongs to the SecD/SecF family. SecD subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01463}.
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DR   EMBL; AE017126; AAP99811.1; -; Genomic_DNA.
DR   RefSeq; NP_875159.1; NC_005042.1.
DR   RefSeq; WP_011124919.1; NC_005042.1.
DR   AlphaFoldDB; Q7VCH3; -.
DR   SMR; Q7VCH3; -.
DR   STRING; 167539.Pro_0767; -.
DR   PRIDE; Q7VCH3; -.
DR   EnsemblBacteria; AAP99811; AAP99811; Pro_0767.
DR   GeneID; 54200116; -.
DR   KEGG; pma:Pro_0767; -.
DR   PATRIC; fig|167539.5.peg.812; -.
DR   eggNOG; COG0342; Bacteria.
DR   HOGENOM; CLU_007894_4_2_3; -.
DR   OMA; MVVYYRL; -.
DR   OrthoDB; 121331at2; -.
DR   Proteomes; UP000001420; 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; IPR001036; Acrflvin-R.
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   PRINTS; PR00702; ACRIFLAVINRP.
DR   TIGRFAMs; TIGR00916; 2A0604s01; 1.
DR   TIGRFAMs; TIGR01129; secD; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Protein transport;
KW   Reference proteome; Translocation; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..494
FT                   /note="Protein translocase subunit SecD"
FT                   /id="PRO_0000412681"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT   TRANSMEM        322..342
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT   TRANSMEM        345..365
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT   TRANSMEM        372..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT   TRANSMEM        420..440
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"
SQ   SEQUENCE   494 AA;  53851 MW;  8F97A232362BAAEE CRC64;
     MARQQGWFAL LIALVISAFL LCINLPFQLG LDLRGGSQLT LEVQALNPNE QIKSEQLEAV
     QSVLDRRVNG LGVAESSLRT IGTNQLILEL PGEQEPSKAA RVLGKTALLE FRKQKINTKS
     EMQRLQRIRS QVNNIDLYKK ASKDNKSELI ENKKIGEQVN DLRVALGLAN SSLNEHDQID
     QIRQKVNSEI VELFEPSSLT GSDLVSAGRR QEQNLTSWEV TLAFNQDGGE KFASLTKSIA
     GSDRLLGIIL DGESISEASV GEQFKVAGIT GGSATISGNF TAESARELEV QLRGGSLPLP
     VSIVQVRTIG PTLGVDNIRR SLIAALLGLS LVAIFMVSFY RLAGFIAIFA LSFYALFNIA
     IYALIPVTLT LPGVAGFVLS IGMAVDANVL IFERVKDELR RGNTLIRSIE TGFSQAFSSI
     IDGHITTLIS CISLFYLGTG FVKGFAATLG IGVFISLFTA LSCTRVLLRF FMSYKSLRKT
     TNFLSENQLP KQLT