ID   GSPL_PECCC              Reviewed;         425 AA.
AC   P31708;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Type II secretion system protein L;
DE            Short=T2SS protein L;
DE   AltName: Full=General secretion pathway protein L;
DE   AltName: Full=Pectic enzymes secretion protein OutL;
GN   Name=outL;
OS   Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp.
OS   carotovora).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SCRI 193;
RX   PubMed=8326859; DOI=10.1111/j.1365-2958.1993.tb01589.x;
RA   Reeves P.J., Whitcombe D., Wharam S., Gibson M., Allison G., Bunce N.,
RA   Barallon R., Douglas P., Mulholland V., Stevens S., Walker S.,
RA   Salmond G.P.C.;
RT   "Molecular cloning and characterization of 13 out genes from Erwinia
RT   carotovora subspecies carotovora: genes encoding members of a general
RT   secretion pathway (GSP) widespread in Gram-negative bacteria.";
RL   Mol. Microbiol. 8:443-456(1993).
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 OutM resulting in a stable complex in the
CC       inner membrane. Provides thus a link between the energy-providing OutE
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. Interacts with OutM/GspM. Interacts with
CC       OutE/GspE and OutF/GspF (By similarity). {ECO:0000250|UniProtKB:P25060,
CC       ECO:0000250|UniProtKB:Q00514}.
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}.
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DR   EMBL; X70049; CAA49653.1; -; Genomic_DNA.
DR   PIR; S32866; S32866.
DR   AlphaFoldDB; P31708; -.
DR   SMR; P31708; -.
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   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Protein transport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..425
FT                   /note="Type II secretion system protein L"
FT                   /id="PRO_0000207315"
FT   TOPO_DOM        1..273
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P25060"
FT   TRANSMEM        274..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        291..425
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P25060"
SQ   SEQUENCE   425 AA;  47640 MW;  3F30DBFE5D82874E CRC64;
     MKIAGKWKRK AAKAPLHRGT VARHPCLIVR LPVEEQGEIE WQVRSSNGES LLSQGRGSIE
     QVRPALAAYP SVTFTRVLVP ATDVTFYALT LPRQARRHVT QVVPFMLEDQ LATEIEKLHF
     AVLEIHGDDG TVAVVEKNRM QRWLAQCDAL GLSVDTLLPD ARVLPKHQDG WSALQHDDMW
     LFRQPTGHAM AAESSWCGDL LKASMPLPAI YSYSAASVGG ELAQYEWQEE GEWKAQPETD
     LFTLAATAHL PASVDLRQGD YAPDKAWQNT LLPWRGVGIA FACYLLLVVA DAGWAHYQLY
     QQAEHWRQES VRVYRQIFPS ETNVVNPRAQ MQQHLQRTAA GGAGKALLDQ LTPLQQLMTQ
     NSAIKIQSLS YDGAAGEFRL ALQGTSYQEL EQFQQQAAAY YQVQAGEMRQ ENDRVEGRLT
     LRSQQ