GSPM_PSEAE
ID GSPM_PSEAE Reviewed; 174 AA.
AC P25061;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Type II secretion system protein M;
DE Short=T2SS protein M;
DE AltName: Full=General secretion pathway protein M;
GN Name=xcpZ; OrderedLocusNames=PA3095;
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 XCPY, 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, DOMAIN, AND INTERACTION WITH XCPY.
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 XCPY; 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 XCPY.
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).
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 XcpY 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 (By similarity). Interacts with XcpY/GspL
CC (PubMed:9884230, PubMed:11872731, PubMed:16168578, PubMed:30337370).
CC Interacts with XcpR/GspE and XcpS/GspF (PubMed:16168578).
CC {ECO:0000250|UniProtKB:P41851, ECO:0000250|UniProtKB:Q00514,
CC ECO:0000269|PubMed:11872731, ECO:0000269|PubMed:16168578,
CC ECO:0000269|PubMed:30337370, ECO:0000269|PubMed:9884230}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:8763961};
CC Single-pass membrane protein {ECO:0000269|PubMed:8763961}.
CC -!- DOMAIN: Two distinct periplasmic domains, one located in the proximity
CC of the transmembrane domain and the other located towards the C-
CC terminal part of the protein are both involved in the interaction with
CC XcpY. {ECO:0000269|PubMed:11872731}.
CC -!- DISRUPTION PHENOTYPE: Absence of XcpZ results in decreased amount of
CC XcpY in type II secretion system complexes.
CC {ECO:0000269|PubMed:9884230}.
CC -!- SIMILARITY: Belongs to the GSP M family. {ECO:0000305}.
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DR EMBL; X56183; CAA39645.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06483.1; -; Genomic_DNA.
DR PIR; G83257; G83257.
DR PIR; S12356; S12356.
DR RefSeq; NP_251785.1; NC_002516.2.
DR RefSeq; WP_003091369.1; NZ_QZGE01000009.1.
DR AlphaFoldDB; P25061; -.
DR SMR; P25061; -.
DR STRING; 287.DR97_4838; -.
DR PaxDb; P25061; -.
DR DNASU; 882766; -.
DR EnsemblBacteria; AAG06483; AAG06483; PA3095.
DR GeneID; 882766; -.
DR KEGG; pae:PA3095; -.
DR PATRIC; fig|208964.12.peg.3247; -.
DR PseudoCAP; PA3095; -.
DR HOGENOM; CLU_118900_2_1_6; -.
DR OMA; QPWRARE; -.
DR BioCyc; PAER208964:G1FZ6-3151-MON; -.
DR Proteomes; UP000002438; Chromosome.
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; 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 Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..174
FT /note="Type II secretion system protein M"
FT /id="PRO_0000207327"
FT TOPO_DOM 1..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8763961"
FT TRANSMEM 33..52
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:8763961"
FT TOPO_DOM 53..174
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:8763961"
SQ SEQUENCE 174 AA; 19265 MW; 78FDC00F36AD22A1 CRC64;
MKVMTQFHER LRAQAETSQL AIRWRGLPAR DRLALLWLGA FLLLVVLYLA LWRPAERHLQ
SARQYFTEQR ALHAYIQQQA PNVRQADAAA PQAQIDPAAL QGMVTASAAQ AGLSVERLDN
EGEGAVQVAL QPAPFAKLLP WLEQLNGQGV QVAEAGLDRQ VDGRVSARLS LRVE
