(data stored in ACNUC10821 zone)

SWISSPROT: C8U1L9_ECO10

ID   C8U1L9_ECO10            Unreviewed;       844 AA.
AC   C8U1L9;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 60.
DE   RecName: Full=Penicillin-binding protein 1B {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|PIRNR:PIRNR002799};
GN   Name=mrcB {ECO:0000313|EMBL:BAI29027.1};
GN   OrderedLocusNames=ECO103_0149 {ECO:0000313|EMBL:BAI29027.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29027.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29027.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: Cell wall formation. Synthesis of cross-linked
CC       peptidoglycan from the lipid intermediates. The enzyme has a
CC       penicillin-insensitive transglycosylase N-terminal domain
CC       (formation of linear glycan strands) and a penicillin-sensitive
CC       transpeptidase C-terminal domain (cross-linking of the peptide
CC       subunits). {ECO:0000256|PIRNR:PIRNR002799}.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|PIRNR:PIRNR002799}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the
CC       transpeptidase family. {ECO:0000256|PIRNR:PIRNR002799}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       glycosyltransferase 51 family. {ECO:0000256|PIRNR:PIRNR002799}.
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DR   EMBL; AP010958; BAI29027.1; -; Genomic_DNA.
DR   RefSeq; WP_000918166.1; NC_013353.1.
DR   CAZy; GT51; Glycosyltransferase Family 51.
DR   EnsemblBacteria; BAI29027; BAI29027; ECO103_0149.
DR   KEGG; eoh:ECO103_0149; -.
DR   HOGENOM; HOG000282711; -.
DR   KO; K05365; -.
DR   OMA; VHGMGLA; -.
DR   BioCyc; ECOL585395:ECO103_RS00765-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0016021; C:integral component of 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:0008233; F:peptidase activity; IEA:InterPro.
DR   GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-UniRule.
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: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; -; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR001264; Glyco_trans_51.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR032730; PBP1b_TM.
DR   InterPro; IPR011813; PBP_1b.
DR   InterPro; IPR036950; PBP_transglycosylase.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   InterPro; IPR028166; UB2H.
DR   Pfam; PF14812; PBP1_TM; 1.
DR   Pfam; PF00912; Transgly; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   Pfam; PF14814; UB2H; 1.
DR   PIRSF; PIRSF002799; PBP_1b; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
DR   TIGRFAMs; TIGR02071; PBP_1b; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U1L9.
DR   SWISS-2DPAGE; C8U1L9.
KW   Cell shape {ECO:0000256|PIRNR:PIRNR002799};
KW   Cell wall biogenesis/degradation {ECO:0000256|PIRNR:PIRNR002799};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Glycosyltransferase {ECO:0000256|PIRNR:PIRNR002799};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Peptidoglycan synthesis {ECO:0000256|PIRNR:PIRNR002799};
KW   Transferase {ECO:0000256|PIRNR:PIRNR002799,
KW   ECO:0000256|SAAS:SAAS01077424, ECO:0000313|EMBL:BAI29027.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     65     86       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        1     79       PBP1_TM. {ECO:0000259|Pfam:PF14812}.
FT   DOMAIN      113    197       UB2H. {ECO:0000259|Pfam:PF14814}.
FT   DOMAIN      209    380       Transgly. {ECO:0000259|Pfam:PF00912}.
FT   DOMAIN      473    714       Transpeptidase. {ECO:0000259|Pfam:
FT                                PF00905}.
FT   ACT_SITE    233    233       Proton donor; for transglycosylase
FT                                activity. {ECO:0000256|PIRSR:PIRSR002799-
FT                                1}.
FT   ACT_SITE    510    510       Acyl-ester intermediate; for
FT                                transpeptidase activity.
FT                                {ECO:0000256|PIRSR:PIRSR002799-1}.
SQ   SEQUENCE   844 AA;  94279 MW;  CEC2230FAC738901 CRC64;
     MAGNDREPIG RKGKPTRPVK QKVSRRRYED DDDYDDYDDY EDEEPMPRKG KGKGKGRKPR
     GKRGWLWLLL KLAIVFAVLI AIYGVYLDQK IRSRIDGKVW QLPAAVYGRM VNLEPDMTIS
     KNEMVKLLEA TQYRQVSKMT RPGEFTVQAN SIEMIRRPFD FPDSKEGQVR ARLTFDGDHL
     ATIVNMENNR QFGFFRLDPR LITMISSPNG EQRLFVPRSG FPDLLVDTLL ATEDRHFYEH
     DGISLYSIGR AVLANLTAGR TVQGASTLTQ QLVKNLFLSS ERSYWRKANE AYMALIMDAR
     YSKDRILELY MNEVYLGQSG DNEIRGFPLA SLYYFGRPVE ELSLDQQALL VGMVKGASIY
     NPWRNPKLAL ERRNLVLRLL QQQQIIDQEL YDMLSARPLG VQPRGGVISP QPAFMQLVRQ
     ELQAKLGDKV KDLSGVKIFT TFDSVAQDAA EKAAVEGIPA LKKQRKLSDL ETAIVVVDRF
     SGEVRAMVGG SEPQFAGYNR AMQARRSIGS LAKPATYLTA LSQPKIYRLN TWIADAPIAL
     RQPNGQVWSP QNDDRRYSES GRVMLVDALT RSMNVPTVNL GMALGLPAVT ETWIKLGVPK
     DQLHPVPAML LGALNLTPIE VAQAFQTIAS GGNRAPLSAL RSVIAEDGKV LYQSFPQAER
     AVPAQAAYLT LWTMQQVVQR GTGRQLGAKY PNLHLAGKTG TTNNNVDTWF AGIDGSTVTI
     TWVGRDNNQP TKLYGASGAM SIYQRYLANQ TPTPLNLVPP EDIADMGVDY DGNFVCSGGM
     RVLPVWTSDP QSLCQQSEMQ QQPSGNPFDQ SSQPQQQPQQ QPAQQEQKDS DGVAGWIKDM
     FGSN
//

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