GSPL_VIBCH
ID GSPL_VIBCH Reviewed; 407 AA.
AC P45782; Q9KNK7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Type II secretion system protein L;
DE Short=T2SS protein L;
DE AltName: Full=Cholera toxin secretion protein EpsL;
DE AltName: Full=General secretion pathway protein L;
GN Name=epsL; OrderedLocusNames=VC_2725;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=El Tor TRH7000;
RA Overbye L.J.;
RT "Organization of the general secretion pathway genes in Vibrio cholerae.";
RL Thesis (1994), Michigan State University, United States.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1-246, AND INTERACTION WITH EPSE.
RX PubMed=15843017; DOI=10.1016/j.jmb.2005.02.061;
RA Abendroth J., Murphy P., Sandkvist M., Bagdasarian M., Hol W.G.;
RT "The X-ray structure of the type II secretion system complex formed by the
RT N-terminal domain of EpsE and the cytoplasmic domain of EpsL of Vibrio
RT cholerae.";
RL J. Mol. Biol. 348:845-855(2005).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 1-246, AND SUBUNIT.
RX PubMed=15533433; DOI=10.1016/j.jmb.2004.09.062;
RA Abendroth J., Bagdasarian M., Sandkvist M., Hol W.G.;
RT "The structure of the cytoplasmic domain of EpsL, an inner membrane
RT component of the type II secretion system of Vibrio cholerae: an unusual
RT member of the actin-like ATPase superfamily.";
RL J. Mol. Biol. 344:619-633(2004).
CC -!- FUNCTION: Inner membrane component of the type II secretion system
CC required for the energy-dependent secretion of extracellular factors
CC such as proteases and toxins from the periplasm. Plays a role in the
CC complex assembly and recruits EpsM resulting in a stable complex in the
CC inner membrane. Provides thus a link between the energy-providing EpsE
CC protein in the cytoplasm and the rest of the T2SS machinery.
CC {ECO:0000250|UniProtKB:P25060}.
CC -!- SUBUNIT: Type II secretion system is composed of four main components:
CC the outer membrane complex, the inner membrane complex, the cytoplasmic
CC secretion ATPase and the periplasm-spanning pseudopilus (By
CC similarity). Forms homodimers (PubMed:15533433). Interacts with
CC EpsM/GspM. Interacts with EpsE/GspE and EpsF/GspF (PubMed:15843017).
CC {ECO:0000250|UniProtKB:Q00514, ECO:0000269|PubMed:15533433,
CC ECO:0000269|PubMed:15843017}.
CC -!- INTERACTION:
CC P45782; P41851: epsM; NbExp=2; IntAct=EBI-6400836, EBI-6400843;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P25060}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P25060}.
CC -!- SIMILARITY: Belongs to the GSP L family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA58793.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L33796; AAA58793.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE003852; AAF95865.1; -; Genomic_DNA.
DR PIR; G82040; G82040.
DR PIR; PN0646; PN0646.
DR RefSeq; NP_232352.1; NC_002505.1.
DR PDB; 1W97; X-ray; 2.70 A; L=1-246.
DR PDB; 1YF5; X-ray; 2.75 A; L=1-246.
DR PDB; 2BH1; X-ray; 2.40 A; A/B=5-246.
DR PDBsum; 1W97; -.
DR PDBsum; 1YF5; -.
DR PDBsum; 2BH1; -.
DR AlphaFoldDB; P45782; -.
DR SMR; P45782; -.
DR IntAct; P45782; 1.
DR STRING; 243277.VC_2725; -.
DR DNASU; 2615553; -.
DR EnsemblBacteria; AAF95865; AAF95865; VC_2725.
DR KEGG; vch:VC_2725; -.
DR PATRIC; fig|243277.26.peg.2600; -.
DR eggNOG; COG3297; Bacteria.
DR HOGENOM; CLU_041016_2_1_6; -.
DR OMA; PLELPMQ; -.
DR BioCyc; VCHO:VC2725-MON; -.
DR EvolutionaryTrace; P45782; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IEA:InterPro.
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:0015627; C:type II protein secretion system complex; IEA:InterPro.
DR GO; GO:0015628; P:protein secretion by the type II secretion system; IEA:InterPro.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR024230; GspL_cyto_dom.
DR InterPro; IPR025691; GspL_pp_dom.
DR InterPro; IPR007812; T2SS_protein-GspL.
DR Pfam; PF12693; GspL_C; 1.
DR Pfam; PF05134; T2SSL; 1.
DR PIRSF; PIRSF015761; Protein_L; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR01709; typeII_sec_gspL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..407
FT /note="Type II secretion system protein L"
FT /id="PRO_0000207319"
FT TOPO_DOM 1..257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P25060"
FT TRANSMEM 258..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..407
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P25060"
FT CONFLICT 336
FT /note="S -> T (in Ref. 1; AAA58793)"
FT /evidence="ECO:0000305"
FT STRAND 7..13
FT /evidence="ECO:0007829|PDB:2BH1"
FT STRAND 19..27
FT /evidence="ECO:0007829|PDB:2BH1"
FT TURN 28..31
FT /evidence="ECO:0007829|PDB:2BH1"
FT STRAND 32..41
FT /evidence="ECO:0007829|PDB:2BH1"
FT HELIX 42..48
FT /evidence="ECO:0007829|PDB:2BH1"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:2BH1"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:2BH1"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:2BH1"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:2BH1"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:2BH1"
FT HELIX 81..89
FT /evidence="ECO:0007829|PDB:2BH1"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:2BH1"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:2BH1"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:2BH1"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:2BH1"
FT STRAND 109..118
FT /evidence="ECO:0007829|PDB:2BH1"
FT HELIX 119..131
FT /evidence="ECO:0007829|PDB:2BH1"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:2BH1"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:2BH1"
FT STRAND 150..158
FT /evidence="ECO:0007829|PDB:2BH1"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:2BH1"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:2BH1"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:2BH1"
FT HELIX 179..183
FT /evidence="ECO:0007829|PDB:2BH1"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:2BH1"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:2BH1"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:2BH1"
FT HELIX 222..230
FT /evidence="ECO:0007829|PDB:2BH1"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:2BH1"
SQ SEQUENCE 407 AA; 45749 MW; 0D408BEC40AF41DB CRC64;
MEGSVSEFLT VRLSSQKEAD IPWLVWSAEQ QEVIASGQVA GWEALHEIES YADQRSVVVL
LAASDLILTS VEIPPGASRQ LENMLPYLLE DEIAQDVEDV HFCVLSKGRE TADVVGVDRL
WLRACLDHLK ACGFDVKRVL PDVLAIPRPE HGLAALQLGD EWLVRKSTTQ GMAVDAQWLS
LLAASDWVQN EGEYLPLQAL TPLPELSLAE TQEWRYEPSG LVMQLLTQEA LTSKFNLLTG
SFKLKSSWLR YWQIWRKVAI AAGLFVAVSI SYSLFQAHQY EAQADAYRAE SERIFRSIFP
DKQKIPTVTY LKRQMSDEMA RLSGGASVGS VLKWLSPLPE ALKGVNLQLQ SIKFDSNRSE
IRLEATSRDF QSFEQARTQL EQYFAVEQGQ LNKNGEQVFG VFVVKPK
