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Database: UniProt
Entry: A8FHY9_BACP2
LinkDB: A8FHY9_BACP2
Original site: A8FHY9_BACP2 
ID   A8FHY9_BACP2            Unreviewed;       355 AA.
AC   A8FHY9;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   24-JAN-2024, entry version 86.
DE   SubName: Full=Glycosyl transferase {ECO:0000313|EMBL:ABV63856.1};
GN   OrderedLocusNames=BPUM_3202 {ECO:0000313|EMBL:ABV63856.1};
OS   Bacillus pumilus (strain SAFR-032).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=315750 {ECO:0000313|EMBL:ABV63856.1, ECO:0000313|Proteomes:UP000001355};
RN   [1] {ECO:0000313|EMBL:ABV63856.1, ECO:0000313|Proteomes:UP000001355}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV63856.1,
RC   ECO:0000313|Proteomes:UP000001355};
RX   PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA   Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA   Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA   Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA   Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA   Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA   Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA   Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA   Weinstock G.M.;
RT   "Paradoxical DNA repair and peroxide resistance gene conservation in
RT   Bacillus pumilus SAFR-032.";
RL   PLoS ONE 2:E928-E928(2007).
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; CP000813; ABV63856.1; -; Genomic_DNA.
DR   RefSeq; WP_003212692.1; NZ_VEIS01000025.1.
DR   AlphaFoldDB; A8FHY9; -.
DR   STRING; 315750.BPUM_3202; -.
DR   GeneID; 69521765; -.
DR   KEGG; bpu:BPUM_3202; -.
DR   eggNOG; COG0472; Bacteria.
DR   HOGENOM; CLU_023982_2_4_9; -.
DR   OMA; MCLGFLP; -.
DR   OrthoDB; 9783652at2; -.
DR   Proteomes; UP000001355; 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; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABV63856.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        50..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        74..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        102..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        135..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        161..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        184..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        214..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        238..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        280..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        313..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         153
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT   BINDING         213
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ   SEQUENCE   355 AA;  38920 MW;  E94F5F5C561AA043 CRC64;
     MDYERALLAF FVSLATVLIV TPIVKKFAIK IGAVDQPNKR KVHDKVMPRM GGLAIFIGVA
     AGALAGGLFL HNKITAISVG AVLIVILGIF DDKYNLSARF KFLVQVLVAC LIVSTGLKMD
     FFSVPFLTDR IELGWMAYPL TVLWIVGITN AINLIDGLDG LAAGISVIGL STIAVMAFSA
     DKILILSLSL VVIGSTIGFL FYNFHPAKIF MGDTGSLFLG YMISVLSLLG LYKSVTLFSV
     VVPVIILGVP IFDTTFAIIR RILNKQPISS PDKSHIHHRL MAFGLSHRMA VIVIYMIGLV
     FSLSAILLTS ATIWLSLIII FLLVMFMQVI AEVTGLVNEE FKPFTKFYKR MVKRQ
//
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