SECY_CHLTR
ID SECY_CHLTR Reviewed; 457 AA.
AC P28539; O84517;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 3.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Protein translocase subunit SecY {ECO:0000255|HAMAP-Rule:MF_01465};
GN Name=secY {ECO:0000255|HAMAP-Rule:MF_01465}; OrderedLocusNames=CT_510;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=L2/434/Bu;
RX PubMed=8202093; DOI=10.1007/bf00280480;
RA Gu L.J., Remacha M., Wenman W.M., Kaul R.;
RT "Cloning and characterization of a secY homolog from Chlamydia
RT trachomatis.";
RL Mol. Gen. Genet. 243:482-487(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-222.
RC STRAIN=L2/434/Bu;
RX PubMed=1735714; DOI=10.1128/jb.174.4.1205-1212.1992;
RA Kaul R., Gray G.J., Koehncke N.R., Gu L.J.;
RT "Cloning and sequence analysis of the Chlamydia trachomatis spc ribosomal
RT protein gene cluster.";
RL J. Bacteriol. 174:1205-1212(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 224-457.
RC STRAIN=L2/434/Bu;
RX PubMed=7730299; DOI=10.1128/jb.177.9.2594-2601.1995;
RA Gu L.J., Wenman W.M., Remacha M., Meuser R.U., Coffin J.M., Kaul R.;
RT "Chlamydia trachomatis RNA polymerase alpha subunit: sequence and
RT structural analysis.";
RL J. Bacteriol. 177:2594-2601(1995).
CC -!- FUNCTION: The central subunit of the protein translocation channel
CC SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two
CC domains form a lateral gate at the front which open onto the bilayer
CC between TMs 2 and 7, and are clamped together by SecE at the back. The
CC channel is closed by both a pore ring composed of hydrophobic SecY
CC resides and a short helix (helix 2A) on the extracellular side of the
CC membrane which forms a plug. The plug probably moves laterally to allow
CC the channel to open. The ring and the pore may move independently.
CC {ECO:0000255|HAMAP-Rule:MF_01465}.
CC -!- SUBUNIT: Component of the Sec protein translocase complex. Heterotrimer
CC consisting of SecY, SecE and SecG subunits. The heterotrimers can form
CC oligomers, although 1 heterotrimer is thought to be able to translocate
CC proteins. Interacts with the ribosome. Interacts with SecDF, and other
CC proteins may be involved. Interacts with SecA. {ECO:0000255|HAMAP-
CC Rule:MF_01465}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. {ECO:0000255|HAMAP-
CC Rule:MF_01465}.
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DR EMBL; L25077; AAC36888.1; -; Unassigned_DNA.
DR EMBL; AE001273; AAC68111.1; -; Genomic_DNA.
DR EMBL; M80325; AAA23180.1; -; Genomic_DNA.
DR EMBL; L33834; AAA74991.1; -; Genomic_DNA.
DR PIR; D71505; D71505.
DR PIR; I40743; I40743.
DR PIR; S44484; S44484.
DR RefSeq; NP_220025.1; NC_000117.1.
DR RefSeq; WP_009871874.1; NC_000117.1.
DR AlphaFoldDB; P28539; -.
DR SMR; P28539; -.
DR STRING; 813.O172_02815; -.
DR EnsemblBacteria; AAC68111; AAC68111; CT_510.
DR GeneID; 884286; -.
DR KEGG; ctr:CT_510; -.
DR PATRIC; fig|272561.5.peg.554; -.
DR HOGENOM; CLU_030313_0_1_0; -.
DR InParanoid; P28539; -.
DR OMA; FAMWLGE; -.
DR Proteomes; UP000000431; Chromosome.
DR GO; GO:0031522; C:cell envelope Sec protein transport complex; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005048; F:signal sequence binding; IBA:GO_Central.
DR GO; GO:0043952; P:protein transport by the Sec complex; IEA:UniProtKB-UniRule.
DR GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IBA:GO_Central.
DR Gene3D; 1.10.3370.10; -; 1.
DR HAMAP; MF_01465; SecY; 1.
DR InterPro; IPR026593; SecY.
DR InterPro; IPR002208; SecY/SEC61-alpha.
DR InterPro; IPR030659; SecY_CS.
DR InterPro; IPR023201; SecY_dom_sf.
DR PANTHER; PTHR10906; PTHR10906; 1.
DR Pfam; PF00344; SecY; 1.
DR PIRSF; PIRSF004557; SecY; 1.
DR SUPFAM; SSF103491; SSF103491; 1.
DR TIGRFAMs; TIGR00967; 3a0501s007; 1.
DR PROSITE; PS00755; SECY_1; 1.
DR PROSITE; PS00756; SECY_2; 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..457
FT /note="Protein translocase subunit SecY"
FT /id="PRO_0000131719"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT VARIANT 55..56
FT /note="QN -> RG (in strain: L2/434/Bu)"
FT VARIANT 173
FT /note="I -> T (in strain: L2/434/Bu)"
FT VARIANT 245
FT /note="M -> I (in strain: L2/434/Bu)"
FT VARIANT 254
FT /note="M -> V (in strain: L2/434/Bu)"
FT VARIANT 401
FT /note="I -> V (in strain: L2/434/Bu)"
FT CONFLICT 221..222
FT /note="GS -> DP (in Ref. 3; AAA23180)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 457 AA; 50303 MW; 74A29F423E19FF11 CRC64;
MATLRQVFSI SELRQKIFFT FSLLALCRIG VFIPVPGING DRAVAYFNQL LGSSQNLFQL
ADIFSGGAFA QMTVIALGVV PYISASIIVQ LLVVFMPTLQ REMRESPDQG KRKLGRMTRL
FTLVLACVQS LLFAKFALRM NLVVPGIVLP AMLSLKLFGV PWVFYLTTVV VMITGTLLLM
WVGEQISDKG IGNGISLIIT LGILASFPSV LGSIFNKLNL GSQDPSEFGI VSLLILCAVF
VFVLMATVLI IEGMRKIPVQ HARRIIGRRE VVGGGSYLPL KVNYAGVIPV IFASSLLMFP
ATIGQFLSSE SSWLKRIATM LSPGSVAYSI FYVLLIIFFT YFWTATQFRP EQIASEMKKN
GAFIPGIRQG KPTQTYLEYT MNRVTLLGAV FLAVVAILPS ILGRILRVDA NVSYFLGGTA
MLIVVGVILD TMKQIDAFLL VRRYDGVLKK DRPKGRP
