(data stored in SCRATCH zone)

SWISSPROT: A0KF71_AERHH

ID   A0KF71_AERHH            Unreviewed;       533 AA.
AC   A0KF71;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 83.
DE   RecName: Full=Peptidoglycan lytic exotransglycosylase {ECO:0000256|SAAS:SAAS00176600};
DE            EC=4.2.2.n1 {ECO:0000256|SAAS:SAAS00176600};
GN   OrderedLocusNames=AHA_0364 {ECO:0000313|EMBL:ABK39556.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK39556.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK39556.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
CC   -!- FUNCTION: Murein-degrading enzyme that degrades murein glycan
CC       strands and insoluble, high-molecular weight murein sacculi, with
CC       the concomitant formation of a 1,6-anhydromuramoyl product. Lytic
CC       transglycosylases (LTs) play an integral role in the metabolism of
CC       the peptidoglycan (PG) sacculus. Their lytic action creates space
CC       within the PG sacculus to allow for its expansion as well as for
CC       the insertion of various structures such as secretion systems and
CC       flagella. {ECO:0000256|SAAS:SAAS00176606}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exolytic cleavage of the (1->4)-beta-glycosidic linkage
CC         between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine
CC         (GlcNAc) residues in peptidoglycan, from either the reducing or
CC         the non-reducing ends of the peptidoglycan chains, with
CC         concomitant formation of a 1,6-anhydrobond in the MurNAc
CC         residue.; EC=4.2.2.n1; Evidence={ECO:0000256|SAAS:SAAS01123190};
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane
CC       {ECO:0000256|SAAS:SAAS00176608}; Peripheral membrane protein
CC       {ECO:0000256|SAAS:SAAS00176608}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the
CC       transglycosylase Slt family. {ECO:0000256|SAAS:SAAS00563655}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the bacterial
CC       solute-binding protein 3 family. {ECO:0000256|SAAS:SAAS00563618}.
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DR   EMBL; CP000462; ABK39556.1; -; Genomic_DNA.
DR   RefSeq; WP_011704342.1; NC_008570.1.
DR   RefSeq; YP_854893.1; NC_008570.1.
DR   STRING; 380703.AHA_0364; -.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   EnsemblBacteria; ABK39556; ABK39556; AHA_0364.
DR   GeneID; 4490810; -.
DR   KEGG; aha:AHA_0364; -.
DR   PATRIC; fig|380703.7.peg.349; -.
DR   eggNOG; ENOG4105CHQ; Bacteria.
DR   eggNOG; COG4623; LUCA.
DR   HOGENOM; HOG000270331; -.
DR   OMA; MEQVGMG; -.
DR   BioCyc; AHYD380703:G1G7B-365-MONOMER; -.
DR   Proteomes; UP000000756; Chromosome.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008933; F:lytic transglycosylase activity; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0000270; P:peptidoglycan metabolic process; IEA:InterPro.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR001638; Solute-binding_3/MltF_N.
DR   InterPro; IPR000189; Transglyc_AS.
DR   InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR   Pfam; PF00497; SBP_bac_3; 1.
DR   Pfam; PF01464; SLT; 1.
DR   SMART; SM00062; PBPb; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
DR   PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0KF71.
DR   SWISS-2DPAGE; A0KF71.
KW   Cell outer membrane {ECO:0000256|SAAS:SAAS00176612};
KW   Cell wall biogenesis/degradation {ECO:0000256|SAAS:SAAS00176607};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000756};
KW   Lyase {ECO:0000256|SAAS:SAAS00176604};
KW   Membrane {ECO:0000256|SAAS:SAAS00176610};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000756}.
FT   DOMAIN      103    341       PBPb. {ECO:0000259|SMART:SM00062}.
SQ   SEQUENCE   533 AA;  59781 MW;  8CEE8E4956E4416A CRC64;
     MGPRSIVSYP TDGFARRESA NRRRSHHGSA LVLRHFPHLY LPPVGLAPAR GEATAGACIM
     RRRWLWGLLA LCALPLLAAD LKPQRLPQPG DLASILQKKE LRALVVYERG FFFFDKGAQH
     GILVNQLQGF ERWLNQTYLA KEKIKLKIIY IPVRQDKLLD YLTEGRGDLV AANMTVTPTR
     REQVTFSNPV IAPIEEWVVS QHSLPTFNRI TQLSGRRVWV RASSSYYESL RQLNWLFREL
     GLPPIYIETV PEYLQDGDLL EMVAAGIIPL TVTDSFKGRI WLGMISGLRA HKLIPLRDNG
     RSAWALRNNS PELLKAVNDY LADAGKRTLY SDMALRRLLA RNDQMSNILA PDPLGRLSTI
     RKVLEQQADK YRLDWLMLAA LAYKESGLNA NIRSERGAVG IMQLLPSTGG EVGIRGARLA
     SLEGNVEAAC RYMRLILDTY FNDPKLDVLN RHLFALAAYN AGPNRVQALR AKAEAAGLDP
     NVWFGNVEQL VANEVGQGPI NYVSTIYKYY VAYRFSLPQL EGKAAAIEAV AQP
//

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