ID A5FUK4_ACICJ Unreviewed; 696 AA.
AC A5FUK4;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Peptidoglycan glycosyltransferase {ECO:0000313|EMBL:ABQ29286.1};
DE EC=2.4.1.129 {ECO:0000313|EMBL:ABQ29286.1};
GN OrderedLocusNames=Acry_0057 {ECO:0000313|EMBL:ABQ29286.1};
OS Acidiphilium cryptum (strain JF-5).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidiphilium.
OX NCBI_TaxID=349163 {ECO:0000313|EMBL:ABQ29286.1, ECO:0000313|Proteomes:UP000000245};
RN [1] {ECO:0000313|EMBL:ABQ29286.1, ECO:0000313|Proteomes:UP000000245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JF-5 {ECO:0000313|EMBL:ABQ29286.1,
RC ECO:0000313|Proteomes:UP000000245};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.;
RT "Complete sequence of chromosome of Acidiphilium cryptum JF-5.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000697; ABQ29286.1; -; Genomic_DNA.
DR RefSeq; WP_011941243.1; NC_009484.1.
DR AlphaFoldDB; A5FUK4; -.
DR STRING; 349163.Acry_0057; -.
DR KEGG; acr:Acry_0057; -.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_009289_6_2_5; -.
DR Proteomes; UP000000245; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.30.450.330; -; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30627:SF1; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE FTSI; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
PE 4: Predicted;
KW Glycosyltransferase {ECO:0000313|EMBL:ABQ29286.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000245};
KW Transferase {ECO:0000313|EMBL:ABQ29286.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 107..219
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 271..562
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 696 AA; 74381 MW; 60AEDAA7056C1BAF CRC64;
MTAPPPRDSL SPRVPGRGGR DAARRAGAPE RGAVPRMEHV RVTSPDLARR AAIGVLHSRL
AAGFAGFVLI YLLLAARVVY VTVVHPVPPD KAAIAAQTPS TTVVLPPPAR AEITDRNGEI
LAVSLPAAAL YANPKQVEDP GVAAREIAAV IPGLDPGFLE ARLADRSRDF VYLDRKLTAS
QELAVNRLGI PGVYFENTER RHYPEGNLAA HILGGVTPDQ RGIAGVEDWF NKRLTSAPGK
PLRLSIDIGA EGIVRQAIWQ AMSDYDAKGA CGIVISARTG RVLAMASVPD YNADDLGSAP
ADARFNRCVS GDYEPGSVFK LQTLSMAINS DMIQPWDRFN TTHPLHVGRF TVTDFEPAHI
WMAVPHILAV SSNIGASRIA TILGPQIQRA WLRKLGFFRR PPIQLPEATP PMYHPKSSWK
LLTTMTVSFG NGIAMSPLQL ISAVVPVVNG GIWYPPTLLD HGKRSAGVRV MSERTSLIMR
KMMRNVVTAP DGTGVYARVP GYLVGGKTGT AQVVGPNGRY LQHLNNASFM AAFPMNDPRY
VVYVVVLQPH ATKQMLPFCH GFTTGGYVAA PAVAQIISRI GPMLGIMPLS GQTLAEAQAA
LSIPLDPPAP PGRLALGPGH LFPPGASKYA YILAHQTPPA NMDVAAHDQA LARTEMWQPL
APAAQTVSLP PAPASSAHTL GHRIMNIALP VTRAGG
//
