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Database: UniProt
Entry: H3SCF3_9BACL
LinkDB: H3SCF3_9BACL
Original site: H3SCF3_9BACL 
ID   H3SCF3_9BACL            Unreviewed;       702 AA.
AC   H3SCF3;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Peptidoglycan glycosyltransferase {ECO:0000313|EMBL:EHQ63227.1};
GN   ORFNames=PDENDC454_05954 {ECO:0000313|EMBL:EHQ63227.1};
OS   Paenibacillus dendritiformis C454.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1131935 {ECO:0000313|EMBL:EHQ63227.1, ECO:0000313|Proteomes:UP000003900};
RN   [1] {ECO:0000313|EMBL:EHQ63227.1, ECO:0000313|Proteomes:UP000003900}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C454 {ECO:0000313|EMBL:EHQ63227.1,
RC   ECO:0000313|Proteomes:UP000003900};
RX   PubMed=22461558; DOI=10.1128/JB.00158-12;
RA   Sirota-Madi A., Olender T., Helman Y., Brainis I., Finkelshtein A.,
RA   Roth D., Hagai E., Leshkowitz D., Brodsky L., Galatenko V., Nikolaev V.,
RA   Gutnick D.L., Lancet D., Ben-Jacob E.;
RT   "Genome Sequence of the Pattern-Forming Social Bacterium Paenibacillus
RT   dendritiformis C454 Chiral Morphotype.";
RL   J. Bacteriol. 194:2127-2128(2012).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the transpeptidase family.
CC       {ECO:0000256|ARBA:ARBA00007171}.
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:EHQ63227.1}.
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DR   EMBL; AHKH01000010; EHQ63227.1; -; Genomic_DNA.
DR   RefSeq; WP_006675704.1; NZ_AHKH01000010.1.
DR   AlphaFoldDB; H3SCF3; -.
DR   STRING; 1131935.PDENDC454_05954; -.
DR   PATRIC; fig|1131935.3.peg.1192; -.
DR   OrthoDB; 9770103at2; -.
DR   Proteomes; UP000003900; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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:SF2; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE MRDA; 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   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003900};
KW   Transferase {ECO:0000313|EMBL:EHQ63227.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        25..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          65..274
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          326..668
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          679..702
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        679..693
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   702 AA;  78645 MW;  6A66C180941A6CC4 CRC64;
     MNHPHHDPEK REVINRRNFS HRLNLFFFVT FAVFSVLIVR LAILQFVEGP SLKEKEAQLG
     YKETPIPPLR GSIYDASGEQ VAYSNSTQSL YFNIEKNYGD PKKAELTDTQ KKNREEAKLL
     AQRLADVFKE YGDPEDKPLT ADAIYNDLMD LSARVNFTYT PRIIKTGLTQ KEVAYFLEHK
     PEFPGIDIVE DSVRHYDPMA VQTVGYLKKF KGVRDNPGYY NDIYNNRATT PSEKQYLDYE
     DVGFDGIELM YQEELRGLNG VKKFPVNVAN RIIGPMELTK PQRGNDIHLT IHRHVQKATE
     EAIMQTLERI RNSSNRSERA PYARTGYAVA MEVDTGNIVA MASMPDYNPN VWRNGSITPE
     DYDQYQYYLM NGAIRDVPAP YEDDKERMKH PGSVVYLGST MKPLSVLIGL QEKLFALGET
     YYDGGYAQFG RVGFETKVWN SGNVGYGRIG ASRALEVSSN AFMVDMIGKR LYSMPAVNGR
     NGLKVWDEYM EAFGLGVPTG SGLPREQAGA KDYLHEAERN NAQSALVYAS FGQQGKYTTL
     QLAQFAATLA NRGTRIKPQL VSKITDGNGQ VVKTFGREEL NKTEIDDAYW NVVEDGMLKV
     NVHGFEGFPY SFYRKTGTSQ MDVSGGRVDN AVFIAYAPAD KPKLAVAVVV PEGGFGSYGA
     APIARAMFDA YDEVYGLTGT PKKKPDELKD EQADTSAGQG TE
//
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