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Database: UniProt
Entry: A0A1S2DEU7_9GAMM
LinkDB: A0A1S2DEU7_9GAMM
Original site: A0A1S2DEU7_9GAMM 
ID   A0A1S2DEU7_9GAMM        Unreviewed;       840 AA.
AC   A0A1S2DEU7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Penicillin-binding protein 1A {ECO:0000256|ARBA:ARBA00018638};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
DE            EC=3.4.16.4 {ECO:0000256|ARBA:ARBA00012448};
GN   ORFNames=BC443_13030 {ECO:0000313|EMBL:OHZ01327.1};
OS   Salinicola sp. MIT1003.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Salinicola.
OX   NCBI_TaxID=1882734 {ECO:0000313|EMBL:OHZ01327.1, ECO:0000313|Proteomes:UP000179615};
RN   [1] {ECO:0000313|EMBL:OHZ01327.1, ECO:0000313|Proteomes:UP000179615}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT1003 {ECO:0000313|EMBL:OHZ01327.1,
RC   ECO:0000313|Proteomes:UP000179615};
RA   Biller S.;
RT   "Membrane vesicles in seawater: heterogeneous DNA content and implications
RT   for viral abundance estimates.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC         transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC         substituents of D-alanine.; EC=3.4.16.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034000};
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}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004249}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004249}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004606}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC       family. {ECO:0000256|ARBA:ARBA00007090}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       glycosyltransferase 51 family. {ECO:0000256|ARBA:ARBA00007739}.
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:OHZ01327.1}.
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DR   EMBL; MCAP01000022; OHZ01327.1; -; Genomic_DNA.
DR   RefSeq; WP_071231853.1; NZ_MCAP01000022.1.
DR   AlphaFoldDB; A0A1S2DEU7; -.
DR   STRING; 1882734.BC443_13030; -.
DR   OrthoDB; 9766909at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000179615; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 2.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR001264; Glyco_trans_51.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR036950; PBP_transglycosylase.
DR   InterPro; IPR031376; PCB_OB.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR   PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR32282:SF27; PENICILLIN-BINDING PROTEIN 1A; 1.
DR   Pfam; PF17092; PCB_OB; 1.
DR   Pfam; PF00912; Transgly; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000179615};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT   DOMAIN          60..233
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          376..466
FT                   /note="Penicillin-binding protein OB-like"
FT                   /evidence="ECO:0000259|Pfam:PF17092"
FT   DOMAIN          470..764
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          320..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          809..840
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        320..348
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        811..825
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   840 AA;  92392 MW;  56F36C9C5EE6B0E3 CRC64;
     MKLFTRLLTT AFWLLLSLCA GMVLAVIGAG LYFAPGLPDV HQLQNYELQT PLRIYTEDDK
     LIGEYGEERR MPVSYDEIPE PLINALLAAE DANFYNHPGV DPKGLLRAAV ELASSGDIQS
     GGSTITMQVA RNYLLTLDQT FTRKIREILL ALQMEQILSK PEILELYVNK IYLGHRSYGI
     AAAANTYYGK PLTDLTLPQY AMIAGLPKAP SSFNPLTNPE RALIRRNWIL YRMRELGSID
     QASYDQAVKA PITASRHTAR SEVDAPYVAE MARAYAVERF GDKAYTDNIR ITTTLDSRLQ
     TEARDALVQG LIDYDTRHGW RGPEEKDVPP SLVEAQDRTE RQGLEEELSE SPEVIETARQ
     AAQSSQATIE GVDGDVSNWL KVLERTPSFG PLQPAIVTAT DGKQMRVLNA DGKVITLDWD
     GLKWARVYHS AKWRGEVPAN AAAIASRGDL VRILKEGDHW RLSQRPGAEG AIVVLDPQTG
     AIEALQGGFS FAASKFNRAI QAQRQVGSNF KPFVYLAALQ EGGMTAATII NDAPVVMSQF
     SGDDWRPENA ERQFQGPTRL RVGLYTSRNL VTIRVLQSLG LDNALNFLER FGFARDRLPH
     GLSLALGSAS LTPLEIANAY AVLANGGFQV SPWYIQKVTQ GSQNTVVEQA NPLVACRDCA
     PGATQTVIDG EPRRIAPRVV EPDALYILRS ILRDVIEHGT GRGALSLDRS DIVGKTGTTN
     DQRDAWFSGF NNSLVATVWV GKDDNTTTAE YGAQAALPIW KAFMGPALEG TPEVIPDAPD
     DIVQVRIDPD TGKRLHDDQP GGISEIFRKD NLPEYQPRGI RPELEDESGS QGTGTYEAIF
//
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