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Database: UniProt
Entry: Q7NI32_GLOVI
LinkDB: Q7NI32_GLOVI
Original site: Q7NI32_GLOVI 
ID   Q7NI32_GLOVI            Unreviewed;       384 AA.
AC   Q7NI32;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2003, sequence version 1.
DT   27-MAR-2024, entry version 111.
DE   SubName: Full=Gll2352 protein {ECO:0000313|EMBL:BAC90293.1};
GN   OrderedLocusNames=gll2352 {ECO:0000313|EMBL:BAC90293.1};
OS   Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Gloeobacterales; Gloeobacteraceae;
OC   Gloeobacter.
OX   NCBI_TaxID=251221 {ECO:0000313|EMBL:BAC90293.1, ECO:0000313|Proteomes:UP000000557};
RN   [1] {ECO:0000313|EMBL:BAC90293.1, ECO:0000313|Proteomes:UP000000557}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29082 / PCC 7421 {ECO:0000313|Proteomes:UP000000557};
RX   PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA   Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA   Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA   Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT   cyanobacterium that lacks thylakoids.";
RL   DNA Res. 10:137-145(2003).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR600715-1};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; BA000045; BAC90293.1; -; Genomic_DNA.
DR   RefSeq; NP_925298.1; NC_005125.1.
DR   RefSeq; WP_011142348.1; NC_005125.1.
DR   AlphaFoldDB; Q7NI32; -.
DR   STRING; 251221.gene:10759849; -.
DR   EnsemblBacteria; BAC90293; BAC90293; BAC90293.
DR   KEGG; gvi:gll2352; -.
DR   PATRIC; fig|251221.4.peg.2390; -.
DR   eggNOG; COG0472; Bacteria.
DR   HOGENOM; CLU_023982_2_3_3; -.
DR   InParanoid; Q7NI32; -.
DR   OrthoDB; 9805475at2; -.
DR   PhylomeDB; Q7NI32; -.
DR   Proteomes; UP000000557; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IBA:GO_Central.
DR   GO; GO:0044038; P:cell wall macromolecule biosynthetic process; IBA:GO_Central.
DR   GO; GO:0071555; P:cell wall organization; IBA:GO_Central.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IBA:GO_Central.
DR   CDD; cd06853; GT_WecA_like; 1.
DR   InterPro; IPR000715; Glycosyl_transferase_4.
DR   InterPro; IPR018480; PNAcMuramoyl-5peptid_Trfase_CS.
DR   PANTHER; PTHR22926; PHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE; 1.
DR   PANTHER; PTHR22926:SF3; UNDECAPRENYL-PHOSPHATE ALPHA-N-ACETYLGLUCOSAMINYL 1-PHOSPHATE TRANSFERASE; 1.
DR   Pfam; PF00953; Glycos_transf_4; 1.
DR   PROSITE; PS01348; MRAY_2; 1.
PE   4: Predicted;
KW   Magnesium {ECO:0000256|PIRSR:PIRSR600715-1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR600715-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000557};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..384
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004288846"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        80..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        114..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        140..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        174..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        203..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        227..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        258..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        280..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        322..350
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        356..375
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         195
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT   BINDING         255
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ   SEQUENCE   384 AA;  40602 MW;  7301025CA1137FAD CRC64;
     MPFLIALVAV ACGWLGATPA AWGAGAVQPG ISGDLLSCAI AFVVATVAVL AITPLVRTVG
     LRQGWGVDRP DERKVHTREM VRLGGVSIFL GITFALLLVW GLGSFGFLPP QKEYEIWGVT
     IGAVLFFFLG LSDDFRSQPA WLRLLVQVGI ATGAWSVGVD VDVLSLPGVG VVKLVWWLSL
     PITILWLVGV VNAINFIDGL DGLAAGVCGI AAVVTFSVTV FTGQWQAALI SAAVAGGALG
     FLRYNFNPAQ IFMGDGGAYF LGFLLGGLSV IGVVKSVTTV ALFIPFCILA VPIFDTASVI
     LQRLRTGDSP FKPDKRHLHH RLLKAGLSHR SVVIVIYALT LWAGSIALAI SGMPAGGTYT
     VLATLLLAYT GWEAWRRSQA SRSS
//
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