GSPL_PSEAE
ID GSPL_PSEAE Reviewed; 382 AA.
AC P25060;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Type II secretion system protein L;
DE Short=T2SS protein L;
DE AltName: Full=General secretion pathway protein L;
GN Name=xcpY; OrderedLocusNames=PA3096;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2124971; DOI=10.1002/j.1460-2075.1990.tb07881.x;
RA Filloux A., Bally M., Ball G., Akrim M., Tommassen J., Lazdunski A.;
RT "Protein secretion in Gram-negative bacteria: transport across the outer
RT membrane involves common mechanisms in different bacteria.";
RL EMBO J. 9:4323-4329(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP TOPOLOGY, AND SUBCELLULAR LOCATION.
RX PubMed=8763961; DOI=10.1128/jb.178.14.4297-4300.1996;
RA Bleves S., Lazdunski A., Filloux A.;
RT "Membrane topology of three Xcp proteins involved in exoprotein transport
RT by Pseudomonas aeruginosa.";
RL J. Bacteriol. 178:4297-4300(1996).
RN [4]
RP DISRUPTION PHENOTYPE, INTERACTION WITH XCPZ, AND FUNCTION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=9884230; DOI=10.1099/00221287-144-12-3379;
RA Michel G., Bleves S., Ball G., Lazdunski A., Filloux A.;
RT "Mutual stabilization of the XcpZ and XcpY components of the secretory
RT apparatus in Pseudomonas aeruginosa.";
RL Microbiology 144:3379-3386(1998).
RN [5]
RP FUNCTION, AND INTERACTION WITH XCPZ.
RX PubMed=11872731; DOI=10.1128/jb.184.6.1779-1782.2002;
RA Robert V., Hayes F., Lazdunski A., Michel G.P.;
RT "Identification of XcpZ domains required for assembly of the secreton of
RT Pseudomonas aeruginosa.";
RL J. Bacteriol. 184:1779-1782(2002).
RN [6]
RP INTERACTION WITH XCPZ; XCPR AND XCPS.
RX PubMed=16168578; DOI=10.1016/j.femsle.2005.08.029;
RA Robert V., Filloux A., Michel G.P.;
RT "Subcomplexes from the Xcp secretion system of Pseudomonas aeruginosa.";
RL FEMS Microbiol. Lett. 252:43-50(2005).
RN [7]
RP FUNCTION, AND INTERACTION WITH XCPZ.
RX PubMed=30337370; DOI=10.1074/jbc.ra117.001127;
RA Michel-Souzy S., Douzi B., Cadoret F., Raynaud C., Quinton L., Ball G.,
RA Voulhoux R.;
RT "Direct interactions between the secreted effector and the T2SS components
RT GspL and GspM reveal a new effector-sensing step during type 2 secretion.";
RL J. Biol. Chem. 293:19441-19450(2018).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 303-382, AND SUBUNIT.
RX PubMed=30425318; DOI=10.1038/s41598-018-34956-w;
RA Fulara A., Vandenberghe I., Read R.J., Devreese B., Savvides S.N.;
RT "Structure and oligomerization of the periplasmic domain of GspL from the
RT type II secretion system of Pseudomonas aeruginosa.";
RL Sci. Rep. 8:16760-16760(2018).
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 XcpZ resulting in a stable complex in the
CC inner membrane. Provides thus a link between the energy-providing XcpR
CC protein in the cytoplasm and the rest of the T2SS machinery.
CC {ECO:0000269|PubMed:11872731, ECO:0000269|PubMed:30337370,
CC ECO:0000269|PubMed:9884230}.
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:30425318). Interacts with
CC XcpZ/GspM (PubMed:9884230, PubMed:11872731, PubMed:16168578,
CC PubMed:30337370). Interacts with XcpR/GspE and XcpS/GspF
CC (PubMed:16168578). {ECO:0000250|UniProtKB:Q00514,
CC ECO:0000269|PubMed:11872731, ECO:0000269|PubMed:16168578,
CC ECO:0000269|PubMed:30337370, ECO:0000269|PubMed:30425318,
CC ECO:0000269|PubMed:9884230}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:8763961};
CC Single-pass membrane protein {ECO:0000269|PubMed:8763961}.
CC -!- DISRUPTION PHENOTYPE: Absence of XcpY results in decreased amount of
CC XcpZ in type II secretion system complexes.
CC {ECO:0000269|PubMed:9884230}.
CC -!- SIMILARITY: Belongs to the GSP L family. {ECO:0000305}.
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DR EMBL; X56183; CAA39644.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06484.1; -; Genomic_DNA.
DR PIR; H83257; H83257.
DR PIR; S12355; S12355.
DR RefSeq; NP_251786.1; NC_002516.2.
DR RefSeq; WP_003103522.1; NZ_QZGE01000009.1.
DR PDB; 5N7L; X-ray; 2.50 A; A=303-382.
DR PDB; 6GHU; X-ray; 2.00 A; A/B=304-381.
DR PDBsum; 5N7L; -.
DR PDBsum; 6GHU; -.
DR AlphaFoldDB; P25060; -.
DR SASBDB; P25060; -.
DR SMR; P25060; -.
DR STRING; 287.DR97_4837; -.
DR PaxDb; P25060; -.
DR PRIDE; P25060; -.
DR EnsemblBacteria; AAG06484; AAG06484; PA3096.
DR GeneID; 882778; -.
DR KEGG; pae:PA3096; -.
DR PATRIC; fig|208964.12.peg.3248; -.
DR PseudoCAP; PA3096; -.
DR HOGENOM; CLU_041016_2_2_6; -.
DR OMA; PLELPMQ; -.
DR BioCyc; PAER208964:G1FZ6-3152-MON; -.
DR Proteomes; UP000002438; Chromosome.
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; IDA:PseudoCAP.
DR GO; GO:0015628; P:protein secretion by the type II secretion system; IDA:PseudoCAP.
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; 1.
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..382
FT /note="Type II secretion system protein L"
FT /id="PRO_0000207318"
FT TOPO_DOM 1..233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8763961"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:8763961"
FT TOPO_DOM 255..382
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:8763961"
FT CONFLICT 266
FT /note="A -> R (in Ref. 1; CAA39644)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="D -> A (in Ref. 1; CAA39644)"
FT /evidence="ECO:0000305"
FT HELIX 306..317
FT /evidence="ECO:0007829|PDB:6GHU"
FT STRAND 323..330
FT /evidence="ECO:0007829|PDB:6GHU"
FT TURN 331..334
FT /evidence="ECO:0007829|PDB:6GHU"
FT STRAND 335..344
FT /evidence="ECO:0007829|PDB:6GHU"
FT HELIX 345..357
FT /evidence="ECO:0007829|PDB:6GHU"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:6GHU"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:6GHU"
FT STRAND 373..380
FT /evidence="ECO:0007829|PDB:6GHU"
SQ SEQUENCE 382 AA; 41319 MW; 630051096C6A522B CRC64;
MSGVSALFLP PASTAGADGE LAVWWVQDGE CRRAPFAQAL AEIRAPWRLY LPVEAVTACA
VNLPTQKARW LRQSLPFAVE EQLADDVEQM HLALGPALAD GRHRVFAVQR TWLAAWLALA
EGAGKAPASL HVDADCLPGE GSCLFWLEER WLLGGSGAVR LACGSEDWPV LRDSCPPPQR
AFAAQEVAPL EGVEVQALAG NPHVWLSEQP LGTDLAQAEF AARQQSSQWR RWRPLLGLVG
LWLVLQWGFT LVQAWQLQRE GDRYAAQSAE LYRQLFPEDR KLINLRAQFD QHLADSASSG
GEGQLLGLLG QAATVIGGEP TVSVEQLDFS AARGDVALQV RAPGFDVLER LRSRLSESGL
AVQLGSASRD GSTVSARLVI GG
