ID   GSPL_AERHY              Reviewed;         389 AA.
AC   P45789;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Type II secretion system protein L;
DE            Short=T2SS protein L;
DE   AltName: Full=General secretion pathway protein L;
GN   Name=exeL;
OS   Aeromonas hydrophila.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=644;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Ah65;
RX   PubMed=8407845; DOI=10.1128/jb.175.20.6695-6703.1993;
RA   Howard S.P., Critch J., Bedi A.;
RT   "Isolation and analysis of eight exe genes and their involvement in
RT   extracellular protein secretion and outer membrane assembly in Aeromonas
RT   hydrophila.";
RL   J. Bacteriol. 175:6695-6703(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 ExeM resulting in a stable complex in the
CC       inner membrane. Provides thus a link between the energy-providing ExeE
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 ExeM/GspM. Interacts with
CC       ExeE/GspE and ExeF/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; X66504; CAA47133.1; -; Genomic_DNA.
DR   PIR; E49905; E49905.
DR   AlphaFoldDB; P45789; -.
DR   SMR; P45789; -.
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..389
FT                   /note="Type II secretion system protein L"
FT                   /id="PRO_0000207313"
FT   TOPO_DOM        1..248
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P25060"
FT   TRANSMEM        249..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P25060"
FT   TOPO_DOM        266..389
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P25060"
SQ   SEQUENCE   389 AA;  42780 MW;  9E8346951D64FDD7 CRC64;
     MAGEIFVSES LVIRLGTNAQ QPVEWLVWSA KEEEIIASGI LASAHALGEL RERAGGRPVV
     TLVPGSDLIF RRVSLPGKYS RQAAAALPYL LEEQIASDVD ELHLVVLGHE GHEVDLMAVD
     KEKMQIWLGW LQQAGLKSQQ LLPDVLALPP AADGWSALQL GKEWLLRQGP CQGIVADESL
     LAMLLAAEAD PVTIHSHTPL PAIPAANWLA ADPELPMLLL AKGALNCQAN LLQGPYRPQT
     EYSRYWLQWR KVAVVAGLLL LVALTQRGMH LYQLAEQDKA LKAEIRQVYT RIFPGENRIV
     NVRSQMAQHL KLLGQTPQDG VLLLLTELAP TFAEVPGLKP QVLRFDAARG ELRLQVTAPG
     FAEIERFREL AGKRFEVQQG EGAQHRGQG