GSPD_XANCP
ID GSPD_XANCP Reviewed; 759 AA.
AC P29041; P31763;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Secretin XpsD;
DE AltName: Full=General secretion pathway protein D;
DE AltName: Full=Type II secretion system protein D;
DE Short=T2SS protein D;
DE Flags: Precursor;
GN Name=xpsD; Synonyms=pefD; OrderedLocusNames=XCC0670;
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1313415; DOI=10.1128/jb.174.8.2679-2687.1992;
RA Hu N.-T., Hung M.-N., Chiou S.-J., Tang F., Chiang D.-C., Huang H.-Y.,
RA Wu C.-Y.;
RT "Cloning and characterization of a gene required for the secretion of
RT extracellular enzymes across the outer membrane by Xanthomonas campestris
RT pv. campestris.";
RL J. Bacteriol. 174:2679-2687(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
RN [3]
RP INTERACTION WITH XPSN.
RX PubMed=10692359; DOI=10.1128/jb.182.6.1549-1557.2000;
RA Lee H.-M., Wang K.-C., Liu Y.-L., Yew H.-Y., Chen L.-Y., Leu W.-M.,
RA Chen D.C., Hu N.-T.;
RT "Association of the cytoplasmic membrane protein XpsN with the outer
RT membrane protein XpsD in the type II protein secretion apparatus of
RT Xanthomonas campestris pv. campestris.";
RL J. Bacteriol. 182:1549-1557(2000).
CC -!- FUNCTION: Involved in a type II secretion system (T2SS, formerly
CC general secretion pathway, GSP) for the export of proteins. This
CC subunit forms the outer membrane channel.
CC {ECO:0000250|UniProtKB:P45779}.
CC -!- SUBUNIT: Forms a cylindrical channel with 15 subunits (By similarity).
CC Binds to XpsN (PubMed:10692359). {ECO:0000250|UniProtKB:P45779,
CC ECO:0000269|PubMed:10692359}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000250|UniProtKB:P45779}. Note=Most of the protein is in the
CC periplasm which it traverses to contact proteins of the cell inner
CC membrane. {ECO:0000250|UniProtKB:P45779}.
CC -!- DOMAIN: The N0, N1, N2 and N3 domains are periplasmic, while the
CC secretin and S domains form a channel that is partially inserted in the
CC outer membrane. The N1, N2 and N3 domains each form a periplasmic ring.
CC The secretin domain forms a double beta-barrel structure; the outer
CC barrel has a diameter of about 110 Angstroms while the inner barrel
CC forms the central gate with a small pore in the closed state.
CC {ECO:0000250|UniProtKB:P45779}.
CC -!- SIMILARITY: Belongs to the bacterial secretin family. GSP D subfamily.
CC {ECO:0000305}.
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DR EMBL; M81648; AAA27615.1; -; Genomic_DNA.
DR EMBL; AE008922; AAM39986.1; -; Genomic_DNA.
DR PIR; C41843; C41843.
DR RefSeq; NP_636062.1; NC_003902.1.
DR RefSeq; WP_011035910.1; NC_003902.1.
DR AlphaFoldDB; P29041; -.
DR SMR; P29041; -.
DR STRING; 340.xcc-b100_3685; -.
DR EnsemblBacteria; AAM39986; AAM39986; XCC0670.
DR KEGG; xcc:XCC0670; -.
DR PATRIC; fig|190485.4.peg.735; -.
DR eggNOG; COG1450; Bacteria.
DR HOGENOM; CLU_006756_1_2_6; -.
DR OMA; QIQVGDN; -.
DR Proteomes; UP000001010; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015627; C:type II protein secretion system complex; IBA:GO_Central.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR GO; GO:0015628; P:protein secretion by the type II secretion system; IEA:InterPro.
DR Gene3D; 3.30.1370.120; -; 3.
DR InterPro; IPR001775; GspD/PilQ.
DR InterPro; IPR005644; NolW-like.
DR InterPro; IPR038591; NolW-like_sf.
DR InterPro; IPR004846; T2SS/T3SS.
DR InterPro; IPR013356; T2SS_GspD.
DR InterPro; IPR004845; T2SS_GspD_CS.
DR Pfam; PF00263; Secretin; 1.
DR Pfam; PF03958; Secretin_N; 2.
DR PRINTS; PR00811; BCTERIALGSPD.
DR TIGRFAMs; TIGR02517; type_II_gspD; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS00875; T2SP_D; 1.
PE 1: Evidence at protein level;
KW Cell outer membrane; Lipoprotein; Membrane; Palmitate; Protein transport;
KW Reference proteome; Signal; Transmembrane; Transmembrane beta strand;
KW Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 22..759
FT /note="Secretin XpsD"
FT /id="PRO_0000013106"
FT REGION 40..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..187
FT /note="N0"
FT /evidence="ECO:0000250|UniProtKB:P45779"
FT REGION 189..253
FT /note="N1"
FT /evidence="ECO:0000250|UniProtKB:P45779"
FT REGION 254..323
FT /note="N2"
FT /evidence="ECO:0000250|UniProtKB:P45779"
FT REGION 326..474
FT /note="N3"
FT /evidence="ECO:0000250|UniProtKB:P45779"
FT REGION 352..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..734
FT /note="Secretin"
FT /evidence="ECO:0000250|UniProtKB:P45779"
FT REGION 736..759
FT /note="S domain"
FT /evidence="ECO:0000250|UniProtKB:P45779"
FT COMPBIAS 42..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 585
FT /note="May serve as a pivot that allows opening of the
FT central gate for substrate egress"
FT /evidence="ECO:0000250|UniProtKB:P45779"
FT LIPID 22
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 22
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 759 AA; 79316 MW; A62DCDD53456EA1A CRC64;
MSERMTPRLF PVSLLIGLLA GCATTPPPDV RRDARLDPQV GAAGATQTTA EQRADGNASA
KPTPVIRRGS GTMINQSAAA APSPTLGMAS SGSATFNFEG ESVQAVVKAI LGDMLGQNYV
IAPGVQGTVT LATPNPVSPA QALNLLEMVL GWNNARMVFS GGRYNIVPAD QALAGTVAPS
TASPSAARGF EVRVVPLKYI SASEMKKVLE PYARPNAIVG TDASRNVITL GGTRAELENY
LRTVQIFDVD WLSGMSVGVF PIQSGKAEKI SADLEKVFGE QSKTPSAGMF RFMPLENANA
VLVITPQPRY LDQIQQWLDR IDSAGGGVRL FSYELKYIKA KDLADRLSEV FGGRGNGGNS
GPSLVPGGVV NMLGNNSGGA DRDESLGSSS GATGGDIGGT SNGSSQSGTS GSFGGSSGSG
MLQLPPSTNQ NGSVTLEVEG DKVGVSAVAE TNTLLVRTSA QAWKSIRDVI EKLDVMPMQV
HIEAQIAEVT LTGRLQYGVN WYFENAVTTP SNADGSGGPN LPSAAGRGIW GDVSGSVTSN
GVAWTFLGKN AAAIISALDQ VTNLRLLQTP SVFVRNNAEA TLNVGSRIPI NSTSINTGLG
SDSSFSSVQY IDTGVILKVR PRVTKDGMVF LDIVQEVSTP GARPAACTAA ATTTVNSAAC
NVDINTRRVK TEAAVQNGDT IMLAGLIDDS TTDGSNGIPF LSKLPVVGAL FGRKTQNSDR
REVIVLITPS IVRNPQDARD LTDEYGSKFK SMRPMDVHK
