GSPM_DICCH
ID GSPM_DICCH Reviewed; 161 AA.
AC Q47422;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 07-OCT-2020, entry version 79.
DE RecName: Full=Type II secretion system protein M;
DE Short=T2SS protein M;
DE AltName: Full=General secretion pathway protein M;
DE AltName: Full=Pectic enzymes secretion protein OutM;
GN Name=outM;
OS Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Dickeya.
OX NCBI_TaxID=556;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=EC16;
RX PubMed=1429461; DOI=10.1128/jb.174.22.7385-7397.1992;
RA Lindeberg M., Collmer A.;
RT "Analysis of eight out genes in a cluster required for pectic enzyme
RT secretion by Erwinia chrysanthemi: sequence comparison with secretion genes
RT from other Gram-negative bacteria.";
RL J. Bacteriol. 174:7385-7397(1992).
RN [2]
RP INTERACTION WITH OUTL/GSPL, AND FUNCTION.
RX PubMed=11266368; DOI=10.1093/embo-reports/kve042;
RA Py B., Loiseau L., Barras F.;
RT "An inner membrane platform in the type II secretion machinery of Gram-
RT negative bacteria.";
RL EMBO Rep. 2:244-248(2001).
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 OutL resulting in a stable complex in the
CC inner membrane (By similarity). Provides thus a link between the
CC energy-providing OutE protein in the cytoplasm and the rest of the T2SS
CC machinery (PubMed:11266368). {ECO:0000250|UniProtKB:P25061,
CC ECO:0000269|PubMed:11266368}.
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 (By similarity). Interacts with OutL/GspL
CC (PubMed:11266368). Interacts with OutE/GspE and OutF/GspF (By
CC similarity). {ECO:0000250|UniProtKB:P25061,
CC ECO:0000250|UniProtKB:P41851, ECO:0000250|UniProtKB:Q00514,
CC ECO:0000269|PubMed:11266368}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P25061}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P25061}.
CC -!- SIMILARITY: Belongs to the GSP M family. {ECO:0000305}.
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DR EMBL; L02214; AAA24840.1; -; Genomic_DNA.
DR PIR; B47755; B47755.
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; IPR007690; T2SS_GspM.
DR InterPro; IPR023229; T2SS_M_periplasmic_sf.
DR Pfam; PF04612; T2SSM; 1.
DR PIRSF; PIRSF006291; GspM; 1.
DR SUPFAM; SSF103054; SSF103054; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Protein transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..161
FT /note="Type II secretion system protein M"
FT /id="PRO_0000207325"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P25061"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..161
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P25061"
SQ SEQUENCE 161 AA; 18622 MW; DDEDD3C69345D920 CRC64;
MNELRRRWQV MSQRERLMAL ACGGLVVLCL LYYLIWAPWQ ESVRQWQMTV ERERQTVRWM
QQQPPRFRRR KVRGGRXPVA ISANGIGAQS AVRYGITVLR MQPQESQVSV TLARSDFNNL
LHWLAELEQK NGVITQGIDV TAVPNSPGIV EVTRLSLERV L
