ID A0A258WVH2_9SPHI Unreviewed; 710 AA.
AC A0A258WVH2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Penicillin-binding protein {ECO:0000313|EMBL:OYZ32208.1};
GN ORFNames=B7Y24_05890 {ECO:0000313|EMBL:OYZ32208.1};
OS Sphingobacteriales bacterium 16-39-50.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX NCBI_TaxID=1970581 {ECO:0000313|EMBL:OYZ32208.1, ECO:0000313|Proteomes:UP000216983};
RN [1] {ECO:0000313|EMBL:OYZ32208.1, ECO:0000313|Proteomes:UP000216983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16-39-50 {ECO:0000313|EMBL:OYZ32208.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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:OYZ32208.1}.
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DR EMBL; NCHA01000003; OYZ32208.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A258WVH2; -.
DR Proteomes; UP000216983; Unassembled WGS sequence.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0016763; F:pentosyltransferase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR011812; Pep_trsgly.
DR PANTHER; PTHR30400:SF0; BIOSYNTHETIC PEPTIDOGLYCAN TRANSGLYCOSYLASE; 1.
DR PANTHER; PTHR30400; MONOFUNCTIONAL BIOSYNTHETIC PEPTIDOGLYCAN TRANSGLYCOSYLASE; 1.
DR Pfam; PF00912; Transgly; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 432..579
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT REGION 685..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..710
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 710 AA; 80370 MW; 4FC7504195312DFA CRC64;
MQISKKQYKI IRIVSISLLG LVLIGGAIAY TKREALLNTA IKKAISKADK EYDLELKIES
AGFVGLSSVS FKNITVVPRG RDSLARILNF RVGVKLFPLI LGDIKLSEIK LDRGIVNLVK
RDSVSNFDFI FRKKKSDEPE EKTEMDLGRL ANSLINQLLY KIPDDMDIRD FEIKFRDDSG
SVSLFTRSAT IDDGNVNSTI LVNRNESVWH VEGTVDPGDK QLDLKLFADN KKVELPYLEK
RFGLKLNFDT AMTEMRGVNR SGSQLEVNGS WRVKNLLVNH SRIAGNDIIV PDASLDADMV
FGKNFVAIDS TSTIHLKNIQ IHPFIKYTLS PSKIYELKLH TEELDAQEIM NSFPKGLFES
LDGIQVAGKL QYNLDFYLDS QNPDSVIFNS RLRNEGFKVL KWGKTNIQKI NSTFVYTPYE
YGKPMRDIII GPENPNFVPI DQISPNLKSA LLTAEDPSFY SHNGFVEASI RSSIITNFKA
KAFKRGGSTI SMQLAKNVYL NRQKTLARKI EEILIVWIME SGKLSTKQRM FETYLNLIEW
GRNVYGIGEA SRYYFDKHPS ELSLGEGIFL ASIVPRPKSG LYRFEGDGSL RSGLSSYFNF
IGGIMARRGL TAADSTGYGF WDVRLKESLR SGIPLNDSLI VDSLLIDDVS EDKDTFLQEI
FGRRKPDTVH VKELNKLKIT PKDTGVINIP SRKERREQRK SERDSKNKNQ
//