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Database: UniProt
Entry: L2F5Z7_9GAMM
LinkDB: L2F5Z7_9GAMM
Original site: L2F5Z7_9GAMM 
ID   L2F5Z7_9GAMM            Unreviewed;       828 AA.
AC   L2F5Z7;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Penicillin-binding protein 1B {ECO:0000256|ARBA:ARBA00018637, ECO:0000256|PIRNR:PIRNR002799};
DE            Short=PBP-1b {ECO:0000256|PIRNR:PIRNR002799};
DE            Short=PBP1b {ECO:0000256|PIRNR:PIRNR002799};
DE   AltName: Full=Murein polymerase {ECO:0000256|ARBA:ARBA00032454, ECO:0000256|PIRNR:PIRNR002799};
GN   ORFNames=MOMA_07176 {ECO:0000313|EMBL:ELA08325.1};
OS   Moraxella macacae 0408225.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Moraxella.
OX   NCBI_TaxID=1230338 {ECO:0000313|EMBL:ELA08325.1, ECO:0000313|Proteomes:UP000023795};
RN   [1] {ECO:0000313|EMBL:ELA08325.1, ECO:0000313|Proteomes:UP000023795}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0408225 {ECO:0000313|EMBL:ELA08325.1,
RC   ECO:0000313|Proteomes:UP000023795};
RX   PubMed=23409273;
RA   Ladner J.T., Whitehouse C.A., Koroleva G.I., Palacios G.F.;
RT   "Genome Sequence of Moraxella macacae 0408225, a Novel Bacterial Species
RT   Isolated from a Cynomolgus Macaque with Epistaxis.";
RL   Genome Announc. 1:E00188-12(2013).
CC   -!- FUNCTION: Cell wall formation. Synthesis of cross-linked peptidoglycan
CC       from the lipid intermediates. The enzyme has a penicillin-insensitive
CC       transglycosylase N-terminal domain (formation of linear glycan strands)
CC       and a penicillin-sensitive transpeptidase C-terminal domain (cross-
CC       linking of the peptide subunits). {ECO:0000256|ARBA:ARBA00002624,
CC       ECO:0000256|PIRNR:PIRNR002799}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC         Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC         (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC         cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC         D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC         diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC         Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC         ChEBI:CHEBI:78435; EC=2.4.1.129;
CC         Evidence={ECO:0000256|ARBA:ARBA00023988};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|PIRNR:PIRNR002799}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC       family. {ECO:0000256|ARBA:ARBA00007090, ECO:0000256|PIRNR:PIRNR002799}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       glycosyltransferase 51 family. {ECO:0000256|ARBA:ARBA00007739,
CC       ECO:0000256|PIRNR:PIRNR002799}.
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:ELA08325.1}.
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DR   EMBL; ANIN01000002; ELA08325.1; -; Genomic_DNA.
DR   RefSeq; WP_009501878.1; NZ_ANIN01000002.1.
DR   AlphaFoldDB; L2F5Z7; -.
DR   STRING; 1230338.MOMA_07176; -.
DR   PATRIC; fig|1230338.3.peg.1527; -.
DR   eggNOG; COG0744; Bacteria.
DR   OrthoDB; 9766909at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000023795; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009274; C:peptidoglycan-based cell wall; IEA:UniProtKB-UniRule.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-UniRule.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-UniRule.
DR   GO; GO:0046677; P:response to antibiotic; IEA:InterPro.
DR   Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   Gene3D; 3.30.2060.10; Penicillin-binding protein 1b domain; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR001264; Glyco_trans_51.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR011813; PBP_1b.
DR   InterPro; IPR036950; PBP_transglycosylase.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   InterPro; IPR028166; UB2H.
DR   NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR   NCBIfam; TIGR02071; PBP_1b; 1.
DR   PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR32282:SF11; PENICILLIN-BINDING PROTEIN 1B; 1.
DR   Pfam; PF00912; Transgly; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   Pfam; PF14814; UB2H; 1.
DR   PIRSF; PIRSF002799; PBP_1b; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW   Cell shape {ECO:0000256|PIRNR:PIRNR002799};
KW   Cell wall biogenesis/degradation {ECO:0000256|PIRNR:PIRNR002799};
KW   Glycosyltransferase {ECO:0000256|PIRNR:PIRNR002799};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Peptidoglycan synthesis {ECO:0000256|PIRNR:PIRNR002799};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000023795};
KW   Transferase {ECO:0000256|PIRNR:PIRNR002799};
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          75..158
FT                   /note="Bifunctional transglycosylase second"
FT                   /evidence="ECO:0000259|Pfam:PF14814"
FT   DOMAIN          171..341
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          439..690
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          791..828
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        195
FT                   /note="Proton donor; for transglycosylase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002799-1"
FT   ACT_SITE        473
FT                   /note="Acyl-ester intermediate; for transpeptidase
FT                   activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002799-1"
SQ   SEQUENCE   828 AA;  92467 MW;  8CD88E1AD6F98D04 CRC64;
     MKLTIFTSPK HAQNRQIKPF ESGSFVLSFI FVVIILISLI VLAVYLIKQD RVITQKFEGK
     RWNLPAKVYS QSLDLQQNSP LTTDELENWL GWLNYQASDD YKSVGTYQKK GNTYYIHTRK
     FNFSNKDVEP KQIIKLQISN DKIVNLQSTE RNESGKIRLE PILIGGIYPD NNEDRIVMQL
     DQIPKALIDA LIATEDRGFF EHHGVSIRGT TRAIYSNLSG GARQGGSTIT QQLIKNFYLN
     SDRTLKRKAN EAIMALLLER HYSKQKILQT YINEITLGQN GNHSINGFGL ASQFYFNRPL
     AELRLDQMAL LVGLAKGPTQ YNPIRYPKLA LQRRNVVLNN MLIMGKIDQK TYDTSSQMPL
     DVVKKPSIGQ SRFPDYLDIV KRELNKSYDA DDLKNEGLRI FTSFNPNVQQ AADKAVDQSL
     KQLKKSNPKR LSQLQSALVS ANPQNGELLA VVGSGSEFTG FNRAVDAKRQ VGSLLKPMIY
     LTGFEQGKYN LASGVDDSAI NISQGKKRWS PSNYGGGSHG IVPLTTALAN SYNQAAVRVG
     MSVGVSNIIT NLQRMGVQKE IPNYPATLLG AVDLSPMDML AVYQVLATGG IKHNIHTIRG
     VVDNEGRVIQ GANFQKHQVI NPVAAYLTNY AMQKVVSNGT AKAALTLGEN LKLAGKTGTT
     NDYRDAWFAG YSGNYVSVVW VGLDNNQTTG LSGANGALPI WINFMRRLKP TPVQLPEPAN
     IQWQWLENAT GELSHQDCPN AIRVPIDTRY SPQNLSSCAN DIHLGQQEAQ LAEQQQLDMQ
     ELYDNEQQRL NHLNNPESDT PSDTHNNHEN NQNRTNTLAD EILQLDSR
//
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