SECD_TREPA
ID SECD_TREPA Reviewed; 583 AA.
AC O83425;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Protein translocase subunit SecD {ECO:0000255|HAMAP-Rule:MF_01463};
GN Name=secD {ECO:0000255|HAMAP-Rule:MF_01463}; OrderedLocusNames=TP_0410;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
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 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; AE000520; AAC65398.1; -; Genomic_DNA.
DR PIR; H71326; H71326.
DR RefSeq; WP_010881858.1; NC_021490.2.
DR AlphaFoldDB; O83425; -.
DR SMR; O83425; -.
DR IntAct; O83425; 9.
DR STRING; 243276.TPANIC_0410; -.
DR EnsemblBacteria; AAC65398; AAC65398; TP_0410.
DR GeneID; 57878936; -.
DR KEGG; tpa:TP_0410; -.
DR eggNOG; COG0342; Bacteria.
DR HOGENOM; CLU_007894_4_3_12; -.
DR OMA; MVVYYRL; -.
DR OrthoDB; 121331at2; -.
DR Proteomes; UP000000811; 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 PANTHER; PTHR30081; PTHR30081; 1.
DR Pfam; PF02355; SecD_SecF; 1.
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..583
FT /note="Protein translocase subunit SecD"
FT /id="PRO_0000095973"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 446..468
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 469..489
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 511..531
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 538..558
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
SQ SEQUENCE 583 AA; 63861 MW; 9A787E64C4CFE1A1 CRC64;
MSKKARFGVV LVVLAACSGF LFPTLQWYFL TDAQTRQRAL SSREQIKEYA VQSAERDLAD
LTRLARAGSD EDISARYAPL VAAARQNLSY SGRPAPSRWT AAALVSAFPV KSEQGFVLYA
RPLMEQTYRE AVLKMKRRQA QAVKLGLDLS GGTSVVIKAD LSEVTKGVPD AERAAIRSEA
MALVLSTLEN RINRFGLSEP VIRRQGEDRV YVEIPGLTDR DRVHSIVMGR GVLAFHLVDD
DATQKLLDHY RNNPQGTFDA AHQLHDLSLV PEHTSVLGVY RKDSYGLDVR DGFLVVKKEP
ALEGRHIRDA TVSSGRANEP LVLFDLDHEG ARIFSELTTK EIGRRLAIVS DGKIRSAPAI
REPITAGSGS ISGFSAEEAQ NLKTALRSAW LNVALEIENQ QVVGASMGEE SIRQGTRALV
WGLCAVLLFM LVWYQEAGVN ACVAQLLNLY IMFGVLSAFN LTLTLSSIAG MILTIGMAVD
ANVVVFERIR EELALGKSRG AAVCSGFERA FWAIMDSNVT TFIAALFLSV LGTGPIKGFA
YSLAIGVVSS VFTALFVSRL MFDYGTEVLH KKTVRIGWRI ARV