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Database: UniProt
Entry: A0A1E4L5T0_9PROT
LinkDB: A0A1E4L5T0_9PROT
Original site: A0A1E4L5T0_9PROT 
ID   A0A1E4L5T0_9PROT        Unreviewed;       409 AA.
AC   A0A1E4L5T0;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   03-MAY-2023, entry version 14.
DE   SubName: Full=MSHA biogenesis protein MshG {ECO:0000313|EMBL:ODU50045.1};
GN   ORFNames=ABS92_04345 {ECO:0000313|EMBL:ODU50045.1};
OS   Thiobacillus sp. SCN 63-374.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Thiobacillaceae; Thiobacillus.
OX   NCBI_TaxID=1660149 {ECO:0000313|EMBL:ODU50045.1, ECO:0000313|Proteomes:UP000094238};
RN   [1] {ECO:0000313|EMBL:ODU50045.1, ECO:0000313|Proteomes:UP000094238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA   Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA   Banfield J.F.;
RT   "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT   unravelled with genome-resolved metagenomics.";
RL   Environ. Microbiol. 17:4929-4941(2015).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the GSP F family.
CC       {ECO:0000256|ARBA:ARBA00005745}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ODU50045.1}.
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DR   EMBL; MEFK01000036; ODU50045.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E4L5T0; -.
DR   Proteomes; UP000094238; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.81.30; Type II secretion system (T2SS), domain F; 2.
DR   InterPro; IPR003004; GspF/PilC.
DR   InterPro; IPR018076; T2SS_GspF_dom.
DR   InterPro; IPR042094; T2SS_GspF_sf.
DR   PANTHER; PTHR30012; GENERAL SECRETION PATHWAY PROTEIN; 1.
DR   PANTHER; PTHR30012:SF4; MSHA BIOGENESIS PROTEIN MSHG; 1.
DR   Pfam; PF00482; T2SSF; 2.
DR   PRINTS; PR00812; BCTERIALGSPF.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        176..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        224..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        380..401
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          74..197
FT                   /note="Type II secretion system protein GspF"
FT                   /evidence="ECO:0000259|Pfam:PF00482"
FT   DOMAIN          277..399
FT                   /note="Type II secretion system protein GspF"
FT                   /evidence="ECO:0000259|Pfam:PF00482"
SQ   SEQUENCE   409 AA;  45009 MW;  61F974574C610453 CRC64;
     MLRFAYTGRT RSGEKAQGIL EADNAAACAS SLLKNGISPV TIQETGQSER RGAKKPKNLN
     LFEPAVQPID VQLFSRQLYT LMRAGVPILR SLSGLLESTT NAAFARVITS LKESLEAGRD
     LSMAMRQHPA VFSPFYVAMV RVGEATGRLD EIFLRMFEHL EFERETRARI REALRYPIFV
     LIAMVVAIAV INVFVIPAFA KVYAGLGAEL PLMTRILIET SRLTIAYGWL MLAGLVLAVM
     GFRLWRATPG GRLLWDRFKL KLPLTGSIML RSTLARFART LALSLRSGIP AAQALSVVAE
     VTDNAWIASR VEQMRNGIER GESVLRTAQN AAVFNPVVLQ MIAVGEETGS IDELMQEVSG
     MYEREVDYEI KTLAARIEPL IIVALGGVVL VLALGVFLPM WDLASVAIK
//
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