YIDC_ECOLI
ID YIDC_ECOLI Reviewed; 548 AA.
AC P25714; Q2M818;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Membrane protein insertase YidC;
DE AltName: Full=Foldase YidC;
DE AltName: Full=Inner membrane protein YidC;
DE AltName: Full=Membrane integrase YidC;
DE AltName: Full=Oxa1Ec;
GN Name=yidC; OrderedLocusNames=b3705, JW3683;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-3.
RC STRAIN=K12;
RX PubMed=2415431; DOI=10.1016/0378-1119(85)90206-9;
RA Hansen F.G., Hansen E.B., Atlung T.;
RT "Physical mapping and nucleotide sequence of the rnpA gene that encodes the
RT protein component of ribonuclease P in Escherichia coli.";
RL Gene 38:85-93(1985).
RN [5]
RP TOPOLOGY.
RC STRAIN=K12/ MC1061 / TOP10F';
RX PubMed=9804807; DOI=10.1074/jbc.273.46.30415;
RA Saaf A., Monne M., de Gier J.W., von Heijne G.;
RT "Membrane topology of the 60-kDa Oxa1p homologue from Escherichia coli.";
RL J. Biol. Chem. 273:30415-30418(1998).
RN [6]
RP FUNCTION IN SEC-DEPENDENT PATHWAY, AND INTERACTION WITH TRANSMEMBRANE
RP SEGMENTS.
RX PubMed=10675323; DOI=10.1093/emboj/19.4.542;
RA Scotti P.A., Urbanus M.L., Brunner J., de Gier J.-W., von Heijne G.,
RA van der Does C., Driessen A.J.M., Oudega B., Luirink J.;
RT "YidC, the Escherichia coli homologue of mitochondrial Oxa1p, is a
RT component of the Sec translocase.";
RL EMBO J. 19:542-549(2000).
RN [7]
RP FUNCTION IN SEC-INDEPENDENT PATHWAY, SUBSTRATES, AND DISRUPTION PHENOTYPE.
RX PubMed=10949305; DOI=10.1038/35020586;
RA Samuelson J.C., Chen M., Jiang F., Moeller I., Wiedmann M., Kuhn A.,
RA Phillips G.J., Dalbey R.E.;
RT "YidC mediates membrane protein insertion in bacteria.";
RL Nature 406:637-641(2000).
RN [8]
RP INTERACTION WITH FTSQ AFTER SECY, AND DISRUPTION PHENOTYPE.
RX PubMed=11415986; DOI=10.1093/embo-reports/kve108;
RA Urbanus M.L., Scotti P.A., Froderberg L., Saaf A., de Gier J.W.,
RA Brunner J., Samuelson J.C., Dalbey R.E., Oudega B., Luirink J.;
RT "Sec-dependent membrane protein insertion: sequential interaction of
RT nascent FtsQ with SecY and YidC.";
RL EMBO Rep. 2:524-529(2001).
RN [9]
RP SRP- AND SEC-DEPENDENT INSERTION INTO MEMBRANES, SUBCELLULAR LOCATION, AND
RP TOPOLOGY.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=11821429; DOI=10.1074/jbc.m200311200;
RA Urbanus M.L., Froederberg L., Drew D., Bjoerk P., de Gier J.-W.,
RA Brunner J., Oudega B., Luirink J.;
RT "Targeting, insertion, and localization of Escherichia coli YidC.";
RL J. Biol. Chem. 277:12718-12723(2002).
RN [10]
RP INTERACTION WITH SECD AND SECF.
RX PubMed=12068816; DOI=10.1046/j.1365-2958.2002.02972.x;
RA Nouwen N., Driessen A.J.M.;
RT "SecDFyajC forms a heterotetrameric complex with YidC.";
RL Mol. Microbiol. 44:1397-1405(2002).
RN [11]
RP FUNCTION.
RX PubMed=12724529; DOI=10.1073/pnas.0636761100;
RA Van Der Laan M., Urbanus M.L., Ten Hagen-Jongman C.M., Nouwen N.,
RA Oudega B., Harms N., Driessen A.J.M., Luirink J.;
RT "A conserved function of YidC in the biogenesis of respiratory chain
RT complexes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5801-5806(2003).
RN [12]
RP MUTAGENESIS OF 23-TRP--LYS-27; 334-TRP--GLN-338; 483-PRO--THR-487 AND
RP GLY-512.
RX PubMed=12707259; DOI=10.1074/jbc.m301008200;
RA Chen M., Xie K., Nouwen N., Driessen A.J., Dalbey R.E.;
RT "Conditional lethal mutations separate the M13 procoat and Pf3 coat
RT functions of YidC: different YidC structural requirements for membrane
RT protein insertion.";
RL J. Biol. Chem. 278:23295-23300(2003).
RN [13]
RP MUTAGENESIS OF ILE-361 AND LEU-436.
RX PubMed=14506280; DOI=10.1074/jbc.m307362200;
RA Jiang F., Chen M., Yi L., de Gier J.-W.L., Kuhn A., Dalbey R.E.;
RT "Defining the regions of Escherichia coli YidC that contribute to
RT activity.";
RL J. Biol. Chem. 278:48965-48972(2003).
RN [14]
RP FUNCTION, AND ATP SYNTHASE SUBUNIT AND SECE AS SUBSTRATES.
RX PubMed=12950181; DOI=10.1021/bi034309h;
RA Yi L., Jiang F., Chen M., Cain B., Bolhuis A., Dalbey R.E.;
RT "YidC is strictly required for membrane insertion of subunits a and c of
RT the F(1)F(0)ATP synthase and SecE of the SecYEG translocase.";
RL Biochemistry 42:10537-10544(2003).
RN [15]
RP FUNCTION IN TARGETING AND/OR TRANSLOCATION OF LIPOPROTEINS.
RX PubMed=15140892; DOI=10.1074/jbc.m403229200;
RA Froderberg L., Houben E.N., Baars L., Luirink J., de Gier J.W.;
RT "Targeting and translocation of two lipoproteins in Escherichia coli via
RT the SRP/Sec/YidC pathway.";
RL J. Biol. Chem. 279:31026-31032(2004).
RN [16]
RP FUNCTION IN FOLDING BUT NOT INSERTION OF LACY, AND DISRUPTION PHENOTYPE.
RX PubMed=15067017; DOI=10.1083/jcb.200402067;
RA Nagamori S., Smirnova I.N., Kaback H.R.;
RT "Role of YidC in folding of polytopic membrane proteins.";
RL J. Cell Biol. 165:53-62(2004).
RN [17]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=BL21-DE3;
RX PubMed=16079137; DOI=10.1074/jbc.m506479200;
RA Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA von Heijne G., Daley D.O.;
RT "Protein complexes of the Escherichia coli cell envelope.";
RL J. Biol. Chem. 280:34409-34419(2005).
RN [18]
RP FUNCTION OF PERIPLASMIC DOMAIN.
RX PubMed=17073462; DOI=10.1021/bi060826z;
RA Xie K., Kiefer D., Nagler G., Dalbey R.E., Kuhn A.;
RT "Different regions of the nonconserved large periplasmic domain of
RT Escherichia coli YidC are involved in the SecF interaction and membrane
RT insertase activity.";
RL Biochemistry 45:13401-13408(2006).
RN [19]
RP INTERACTION WITH FTSH.
RX PubMed=18387365; DOI=10.1016/j.febslet.2008.02.082;
RA van Bloois E., Dekker H.L., Froderberg L., Houben E.N., Urbanus M.L.,
RA de Koster C.G., de Gier J.W., Luirink J.;
RT "Detection of cross-links between FtsH, YidC, HflK/C suggests a linked role
RT for these proteins in quality control upon insertion of bacterial inner
RT membrane proteins.";
RL FEBS Lett. 582:1419-1424(2008).
RN [20]
RP COMPLEMENTATION BY AND IN STREPTOCOCCUS MUTANS.
RX PubMed=18178746; DOI=10.1128/jb.01366-07;
RA Dong Y., Palmer S.R., Hasona A., Nagamori S., Kaback H.R., Dalbey R.E.,
RA Brady L.J.;
RT "Functional overlap but lack of complete cross-complementation of
RT Streptococcus mutans and Escherichia coli YidC orthologs.";
RL J. Bacteriol. 190:2458-2469(2008).
RN [21]
RP FUNCTION IN FOLDING BUT NOT INSERTION OF MALF OR OF MALFGK(2) COMPLEX.
RX PubMed=18456666; DOI=10.1074/jbc.m801481200;
RA Wagner S., Pop O.I., Haan G.J., Baars L., Koningstein G., Klepsch M.M.,
RA Genevaux P., Luirink J., de Gier J.W.;
RT "Biogenesis of MalF and the MalFGK(2) maltose transport complex in
RT Escherichia coli requires YidC.";
RL J. Biol. Chem. 283:17881-17890(2008).
RN [22]
RP COMPLEMENTATION BY SPOIIIJ AND YQJG OF B.SUBTILIS.
RX PubMed=19717609; DOI=10.1128/jb.00853-09;
RA Saller M.J., Fusetti F., Driessen A.J.;
RT "Bacillus subtilis SpoIIIJ and YqjG function in membrane protein
RT biogenesis.";
RL J. Bacteriol. 191:6749-6757(2009).
RN [23]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=21778229; DOI=10.1074/jbc.m111.245696;
RA Fontaine F., Fuchs R.T., Storz G.;
RT "Membrane localization of small proteins in Escherichia coli.";
RL J. Biol. Chem. 286:32464-32474(2011).
RN [24]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=BL21-DE3;
RX PubMed=27435098; DOI=10.1042/bcj20160545;
RA Komar J., Alvira S., Schulze R.J., Martin R., Lycklama a Nijeholt J.A.,
RA Lee S.C., Dafforn T.R., Deckers-Hebestreit G., Berger I., Schaffitzel C.,
RA Collinson I.;
RT "Membrane protein insertion and assembly by the bacterial holo-translocon
RT SecYEG-SecDF-YajC-YidC.";
RL Biochem. J. 473:3341-3354(2016).
RN [25] {ECO:0007744|PDB:3BLC}
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 26-340.
RC STRAIN=K12;
RX PubMed=18093969; DOI=10.1074/jbc.m708936200;
RA Oliver D.C., Paetzel M.;
RT "Crystal structure of the major periplasmic domain of the bacterial
RT membrane protein assembly facilitator YidC.";
RL J. Biol. Chem. 283:5208-5216(2008).
RN [26] {ECO:0007744|PDB:3BS6}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 56-329.
RX PubMed=18234665; DOI=10.1074/jbc.m710493200;
RA Ravaud S., Stjepanovic G., Wild K., Sinning I.;
RT "The crystal structure of the periplasmic domain of the Escherichia coli
RT membrane protein insertase YidC contains a substrate binding cleft.";
RL J. Biol. Chem. 283:9350-9358(2008).
RN [27]
RP REVIEW.
RX PubMed=21275640; DOI=10.1146/annurev-biochem-060409-092524;
RA Dalbey R.E., Wang P., Kuhn A.;
RT "Assembly of bacterial inner membrane proteins.";
RL Annu. Rev. Biochem. 80:161-187(2011).
CC -!- FUNCTION: Inner membrane protein required for the insertion and/or
CC proper folding and/or complex formation of integral inner membrane
CC proteins. Involved in integration of membrane proteins that insert
CC dependently and independently of the Sec translocase complex, as well
CC as at least 2 lipoproteins. Its own insertion requires SRP and is Sec
CC translocase-dependent. Essential for the integration of Sec-dependent
CC subunit a of the F(0)ATP synthase, FtsQ and SecE proteins and for Sec-
CC independent subunit c of the F(0)ATP synthase, M13 phage procoat and
CC the N-terminus of leader peptidase Lep. Probably interacts directly
CC with Sec-independent substrates. Sec-dependent protein FtsQ interacts
CC first with SecY then subsequently with YidC. Sec-dependent LacY and
CC MalF require YidC to acquire tertiary structure and stability, a
CC chaperone-like function, but not for membrane insertion. Stable maltose
CC transport copmplex formation (MalFGK(2)) also requires YidC. Partially
CC complements a Streptococcus mutans yidC2 disruption mutant.
CC {ECO:0000269|PubMed:10675323, ECO:0000269|PubMed:10949305,
CC ECO:0000269|PubMed:12724529, ECO:0000269|PubMed:12950181,
CC ECO:0000269|PubMed:15067017, ECO:0000269|PubMed:15140892,
CC ECO:0000269|PubMed:17073462, ECO:0000269|PubMed:18456666}.
CC -!- SUBUNIT: Interacts with SecD and SecF. Component of the SecDF-YajC
CC complex, a heterotetrameric translocase complex. The SecDF-YidC-YajC
CC translocase forms a supercomplex with SecYEG, called the holo-
CC translocon (HTL) (PubMed:27435098). The stoichiometry of the super
CC complex may be SecYEG:YidC:SecDF 4:3:1, YajC is in the reconstituted
CC complex (with SecDF) but as no antibody is available it could not be
CC quantified (PubMed:27435098). Specifically interacts with transmembrane
CC segments of nascent integral membrane proteins during membrane
CC integration. Found in 3 different complexes in inner membrane
CC preparations (PubMed:16079137). Can be cross-linked to FtsH, in the
CC larger FtsH/HflKC complex. {ECO:0000269|PubMed:10675323,
CC ECO:0000269|PubMed:11415986, ECO:0000269|PubMed:12068816,
CC ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:18387365,
CC ECO:0000269|PubMed:27435098}.
CC -!- INTERACTION:
CC P25714; P03623: VIII; Xeno; NbExp=5; IntAct=EBI-6400779, EBI-8482910;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:11821429,
CC ECO:0000269|PubMed:16079137}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11821429, ECO:0000269|PubMed:16079137}.
CC Note=Predominantly localized at cell poles at all stages of cell
CC growth.
CC -!- INDUCTION: At mid-exponential phase in strain MC4100 there are about
CC 2500 copies per cell (at protein level).
CC -!- DOMAIN: Most of the large periplasmic domain (residues 24-264) is not
CC required for either Sec-dependent or Sec-independent protein insertion.
CC However, residues 265-346, the C-terminal part of the large periplasmic
CC domain, are required for both Sec-dependent and Sec-independent protein
CC insertion.
CC -!- DISRUPTION PHENOTYPE: Lethality. Upon depletion experiments insertion
CC of Sec translocase-independent integral membrane proteins ceases.
CC Translocation of Sec-dependent protein decreases to a lesser extent.
CC Also leads to decreased targeting and/or translocation of Lpp and BRP
CC lipoproteins. Both spoIIIJ and yqjG of B.subtilis functionally
CC complement yidC depletion, whereas Streptococcus mutans yidC1 and yidC2
CC only partially complement depletion. {ECO:0000269|PubMed:10949305,
CC ECO:0000269|PubMed:11415986, ECO:0000269|PubMed:15067017,
CC ECO:0000269|PubMed:21778229}.
CC -!- SIMILARITY: Belongs to the OXA1/ALB3/YidC family. Type 1 subfamily.
CC {ECO:0000305}.
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DR EMBL; L10328; AAA62056.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76728.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77588.1; -; Genomic_DNA.
DR EMBL; M11056; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; B65173; B65173.
DR RefSeq; NP_418161.1; NC_000913.3.
DR RefSeq; WP_000378250.1; NZ_SSZK01000035.1.
DR PDB; 3BLC; X-ray; 2.50 A; A/B=26-340.
DR PDB; 3BS6; X-ray; 1.80 A; A/B=56-329.
DR PDB; 4UTQ; EM; 8.00 A; A=1-548.
DR PDB; 5M5H; EM; 4.50 A; A=1-540.
DR PDB; 5MG3; EM; 14.00 A; C=2-548.
DR PDB; 6AL2; X-ray; 2.80 A; A/B=1-540.
DR PDBsum; 3BLC; -.
DR PDBsum; 3BS6; -.
DR PDBsum; 4UTQ; -.
DR PDBsum; 5M5H; -.
DR PDBsum; 5MG3; -.
DR PDBsum; 6AL2; -.
DR AlphaFoldDB; P25714; -.
DR SMR; P25714; -.
DR BioGRID; 4261511; 290.
DR ComplexPortal; CPX-1095; Holo-translocon SecYEG-SecDF-YajC-YidC complex.
DR DIP; DIP-12442N; -.
DR IntAct; P25714; 31.
DR MINT; P25714; -.
DR STRING; 511145.b3705; -.
DR TCDB; 2.A.9.3.1; the membrane protein insertase (yidc/alb3/oxa1) family.
DR jPOST; P25714; -.
DR PaxDb; P25714; -.
DR PRIDE; P25714; -.
DR DNASU; 948214; -.
DR EnsemblBacteria; AAC76728; AAC76728; b3705.
DR EnsemblBacteria; BAE77588; BAE77588; BAE77588.
DR GeneID; 948214; -.
DR KEGG; ecj:JW3683; -.
DR KEGG; eco:b3705; -.
DR PATRIC; fig|1411691.4.peg.2998; -.
DR EchoBASE; EB1183; -.
DR eggNOG; COG0706; Bacteria.
DR HOGENOM; CLU_016535_3_0_6; -.
DR InParanoid; P25714; -.
DR OMA; INPVAGC; -.
DR PhylomeDB; P25714; -.
DR BioCyc; EcoCyc:YIDC; -.
DR BioCyc; MetaCyc:YIDC; -.
DR EvolutionaryTrace; P25714; -.
DR PRO; PR:P25714; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0031522; C:cell envelope Sec protein transport complex; IDA:EcoCyc.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032977; F:membrane insertase activity; IDA:EcoCyc.
DR GO; GO:0006457; P:protein folding; IMP:UniProtKB.
DR GO; GO:0051205; P:protein insertion into membrane; IDA:EcoliWiki.
DR GO; GO:0032978; P:protein insertion into membrane from inner side; IDA:ComplexPortal.
DR GO; GO:0043952; P:protein transport by the Sec complex; IDA:ComplexPortal.
DR GO; GO:0065003; P:protein-containing complex assembly; IMP:UniProtKB.
DR Gene3D; 2.70.98.90; -; 1.
DR HAMAP; MF_01810; YidC_type1; 1.
DR InterPro; IPR019998; Membr_insert_YidC.
DR InterPro; IPR028055; Membr_insert_YidC/Oxa1_C.
DR InterPro; IPR028053; Membr_insert_YidC_N.
DR InterPro; IPR001708; YidC/ALB3/OXA1/COX18.
DR InterPro; IPR038210; YidC_periplasmic.
DR InterPro; IPR038221; YidC_periplasmic_sf.
DR PANTHER; PTHR12428; PTHR12428; 1.
DR Pfam; PF02096; 60KD_IMP; 1.
DR Pfam; PF14849; YidC_periplas; 1.
DR PRINTS; PR00701; 60KDINNERMP.
DR PRINTS; PR01900; YIDCPROTEIN.
DR TIGRFAMs; TIGR03593; yidC_nterm; 1.
DR TIGRFAMs; TIGR03592; yidC_oxa1_cterm; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Chaperone; Membrane;
KW Protein transport; Reference proteome; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..548
FT /note="Membrane protein insertase YidC"
FT /id="PRO_0000124712"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 6..23
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 24..342
FT /note="Periplasmic"
FT TRANSMEM 343..370
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 371..416
FT /note="Cytoplasmic"
FT TRANSMEM 417..446
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 447..463
FT /note="Periplasmic"
FT TRANSMEM 464..481
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 482..493
FT /note="Cytoplasmic"
FT TRANSMEM 494..509
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 510..512
FT /note="Periplasmic"
FT TRANSMEM 513..535
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 536..548
FT /note="Cytoplasmic"
FT REGION 24..264
FT /note="Can be removed without causing lethality,
FT dispensible for M13 procoat processing"
FT REGION 28..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..265
FT /note="Interaction with SecF; not required for insertion of
FT a number of Sec-dependent or Sec-independent substrates"
FT REGION 265..346
FT /note="Required for Sec-dependent and Sec-independent
FT protein insertion"
FT REGION 527..548
FT /note="Can be removed without causing lethality,
FT dispensible for M13 procoat processing"
FT COMPBIAS 28..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 24..27
FT /note="EQDK->IEGR: Cold-sensitive at 30 degrees Celsius;
FT when associated with 334-W--G-338. Protein accumulates
FT stably."
FT MUTAGEN 334..338
FT /note="WFISQ->LEVLFQG: Cold-sensitive at 30 degrees
FT Celsius; when associated with 24-I--R-27. Protein
FT accumulates stably."
FT /evidence="ECO:0000269|PubMed:12707259"
FT MUTAGEN 361
FT /note="I->S: Loss of function."
FT /evidence="ECO:0000269|PubMed:14506280"
FT MUTAGEN 436
FT /note="L->S: Loss of function."
FT /evidence="ECO:0000269|PubMed:14506280"
FT MUTAGEN 483..487
FT /note="PTTVT->LVPRGS: Temperature-sensitive at 42 degrees
FT Celsius; when associated with 512-ENLYFQG. Protein is not
FT stable."
FT /evidence="ECO:0000269|PubMed:12707259"
FT MUTAGEN 512
FT /note="G->ENLYFQG: Temperature-sensitive at 42 degrees
FT Celsius; when associated with 483-L--S-487. Protein is not
FT stable."
FT /evidence="ECO:0000269|PubMed:12707259"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:3BS6"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:3BS6"
FT STRAND 78..90
FT /evidence="ECO:0007829|PDB:3BS6"
FT STRAND 95..103
FT /evidence="ECO:0007829|PDB:3BS6"
FT STRAND 106..116
FT /evidence="ECO:0007829|PDB:3BS6"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:3BS6"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:3BS6"
FT STRAND 145..154
FT /evidence="ECO:0007829|PDB:3BS6"
FT STRAND 160..168
FT /evidence="ECO:0007829|PDB:3BS6"
FT STRAND 173..181
FT /evidence="ECO:0007829|PDB:3BS6"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:3BS6"
FT STRAND 188..201
FT /evidence="ECO:0007829|PDB:3BS6"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:6AL2"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:6AL2"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:3BS6"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:3BS6"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:3BS6"
FT HELIX 235..239
FT /evidence="ECO:0007829|PDB:3BS6"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:3BS6"
FT STRAND 252..257
FT /evidence="ECO:0007829|PDB:3BS6"
FT STRAND 260..280
FT /evidence="ECO:0007829|PDB:3BS6"
FT STRAND 283..289
FT /evidence="ECO:0007829|PDB:3BS6"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:3BS6"
FT STRAND 300..311
FT /evidence="ECO:0007829|PDB:3BS6"
FT HELIX 314..320
FT /evidence="ECO:0007829|PDB:3BS6"
FT HELIX 324..327
FT /evidence="ECO:0007829|PDB:3BS6"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:6AL2"
FT HELIX 334..351
FT /evidence="ECO:0007829|PDB:6AL2"
FT HELIX 354..368
FT /evidence="ECO:0007829|PDB:6AL2"
FT HELIX 370..385
FT /evidence="ECO:0007829|PDB:6AL2"
FT HELIX 387..397
FT /evidence="ECO:0007829|PDB:6AL2"
FT HELIX 401..414
FT /evidence="ECO:0007829|PDB:6AL2"
FT HELIX 421..423
FT /evidence="ECO:0007829|PDB:6AL2"
FT HELIX 424..442
FT /evidence="ECO:0007829|PDB:6AL2"
FT HELIX 444..446
FT /evidence="ECO:0007829|PDB:6AL2"
FT HELIX 466..481
FT /evidence="ECO:0007829|PDB:6AL2"
FT HELIX 489..506
FT /evidence="ECO:0007829|PDB:6AL2"
FT HELIX 511..531
FT /evidence="ECO:0007829|PDB:6AL2"
SQ SEQUENCE 548 AA; 61526 MW; 95EBC5DAB4F2FCFB CRC64;
MDSQRNLLVI ALLFVSFMIW QAWEQDKNPQ PQAQQTTQTT TTAAGSAADQ GVPASGQGKL
ISVKTDVLDL TINTRGGDVE QALLPAYPKE LNSTQPFQLL ETSPQFIYQA QSGLTGRDGP
DNPANGPRPL YNVEKDAYVL AEGQNELQVP MTYTDAAGNT FTKTFVLKRG DYAVNVNYNV
QNAGEKPLEI SSFGQLKQSI TLPPHLDTGS SNFALHTFRG AAYSTPDEKY EKYKFDTIAD
NENLNISSKG GWVAMLQQYF ATAWIPHNDG TNNFYTANLG NGIAAIGYKS QPVLVQPGQT
GAMNSTLWVG PEIQDKMAAV APHLDLTVDY GWLWFISQPL FKLLKWIHSF VGNWGFSIII
ITFIVRGIMY PLTKAQYTSM AKMRMLQPKI QAMRERLGDD KQRISQEMMA LYKAEKVNPL
GGCFPLLIQM PIFLALYYML MGSVELRQAP FALWIHDLSA QDPYYILPIL MGVTMFFIQK
MSPTTVTDPM QQKIMTFMPV IFTVFFLWFP SGLVLYYIVS NLVTIIQQQL IYRGLEKRGL
HSREKKKS
