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Database: UniProt
Entry: A0A934TD74_9BACT
LinkDB: A0A934TD74_9BACT
Original site: A0A934TD74_9BACT 
ID   A0A934TD74_9BACT        Unreviewed;       121 AA.
AC   A0A934TD74;
DT   22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2023, sequence version 1.
DT   02-APR-2025, entry version 10.
DE   RecName: Full=Protein-export membrane protein SecG {ECO:0000256|RuleBase:RU365087};
GN   Name=secG {ECO:0000313|EMBL:MBK5721522.1};
GN   ORFNames=JGH11_11625 {ECO:0000313|EMBL:MBK5721522.1};
OS   Dysgonomonas sp. Marseille-P4677.
OC   Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
OC   Dysgonomonadaceae; Dysgonomonas.
OX   NCBI_TaxID=2364790 {ECO:0000313|EMBL:MBK5721522.1, ECO:0000313|Proteomes:UP000629836};
RN   [1] {ECO:0000313|EMBL:MBK5721522.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=P4677 {ECO:0000313|EMBL:MBK5721522.1};
RA   Hasni I.;
RT   "Description of Dysgonomonas phocaeensis P4677.";
RL   Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in protein export. Participates in an early event of
CC       protein translocation. {ECO:0000256|RuleBase:RU365087}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651,
CC       ECO:0000256|RuleBase:RU365087}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU365087}.
CC   -!- SIMILARITY: Belongs to the SecG family. {ECO:0000256|ARBA:ARBA00008445,
CC       ECO:0000256|RuleBase:RU365087}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU365087}.
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:MBK5721522.1}.
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DR   EMBL; JAEPKU010000062; MBK5721522.1; -; Genomic_DNA.
DR   RefSeq; WP_201111894.1; NZ_JAEPKU010000062.1.
DR   Proteomes; UP000629836; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015450; F:protein-transporting ATPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:TreeGrafter.
DR   GO; GO:0009306; P:protein secretion; IEA:UniProtKB-UniRule.
DR   GO; GO:0043952; P:protein transport by the Sec complex; IEA:TreeGrafter.
DR   InterPro; IPR004692; SecG.
DR   NCBIfam; TIGR00810; secG; 1.
DR   PANTHER; PTHR34182; PROTEIN-EXPORT MEMBRANE PROTEIN SECG; 1.
DR   PANTHER; PTHR34182:SF1; PROTEIN-EXPORT MEMBRANE PROTEIN SECG; 1.
DR   Pfam; PF03840; SecG; 1.
DR   PRINTS; PR01651; SECGEXPORT.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|RuleBase:RU365087};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365087};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW   ECO:0000256|RuleBase:RU365087};
KW   Reference proteome {ECO:0000313|Proteomes:UP000629836};
KW   Translocation {ECO:0000256|ARBA:ARBA00023010,
KW   ECO:0000256|RuleBase:RU365087};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU365087};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU365087};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365087}.
FT   TRANSMEM        53..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365087"
FT   REGION          82..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..105
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..115
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   121 AA;  12357 MW;  773929217707CA30 CRC64;
     MITLITVLIV IAAIALILIV LVQNSKGGGL SSGFSSSNAI MGVRKTTDFL EKATWGLAGF
     IMVMSIVCVM LKPKASSALQ PEIGAPAPVN TNAPDLSTTL PTIPSNTPAA PANEPTTPPA
     E
//
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