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Database: UniProt
Entry: F7QHA6_9BRAD
LinkDB: F7QHA6_9BRAD
Original site: F7QHA6_9BRAD 
ID   F7QHA6_9BRAD            Unreviewed;       544 AA.
AC   F7QHA6;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=peptidoglycan lytic exotransglycosylase {ECO:0000256|ARBA:ARBA00012587};
DE            EC=4.2.2.n1 {ECO:0000256|ARBA:ARBA00012587};
DE   AltName: Full=Murein hydrolase A {ECO:0000256|ARBA:ARBA00030918};
GN   ORFNames=CSIRO_0933 {ECO:0000313|EMBL:EGP09395.1};
OS   Bradyrhizobiaceae bacterium SG-6C.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae.
OX   NCBI_TaxID=709797 {ECO:0000313|EMBL:EGP09395.1, ECO:0000313|Proteomes:UP000003148};
RN   [1] {ECO:0000313|EMBL:EGP09395.1, ECO:0000313|Proteomes:UP000003148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG-6C {ECO:0000313|EMBL:EGP09395.1,
RC   ECO:0000313|Proteomes:UP000003148};
RX   PubMed=21742875; DOI=10.1128/JB.05647-11;
RA   Pearce S.L., Pandey R., Dorrian S.J., Russell R.J., Oakeshott J.G.,
RA   Pandey G.;
RT   "Genome Sequence of the Newly Isolated Chemolithoautotrophic
RT   Bradyrhizobiaceae Strain SG-6C.";
RL   J. Bacteriol. 193:5057-5057(2011).
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 the
CC         non-reducing ends of the peptidoglycan chains, with concomitant
CC         formation of a 1,6-anhydrobond in the MurNAc residue.; EC=4.2.2.n1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001420};
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:EGP09395.1}.
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DR   EMBL; AFOF01000013; EGP09395.1; -; Genomic_DNA.
DR   AlphaFoldDB; F7QHA6; -.
DR   STRING; 709797.CSIRO_0933; -.
DR   eggNOG; COG2821; Bacteria.
DR   HOGENOM; CLU_037751_0_0_5; -.
DR   Proteomes; UP000003148; Chromosome.
DR   GO; GO:0019867; C:outer membrane; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009254; P:peptidoglycan turnover; IEA:InterPro.
DR   CDD; cd14668; mlta_B; 1.
DR   CDD; cd14485; mltA_like_LT_A; 1.
DR   Gene3D; 2.40.240.50; Barwin-like endoglucanases; 1.
DR   Gene3D; 2.40.40.10; RlpA-like domain; 1.
DR   InterPro; IPR010611; 3D_dom.
DR   InterPro; IPR026044; MltA.
DR   InterPro; IPR005300; MltA_B.
DR   InterPro; IPR036908; RlpA-like_sf.
DR   PANTHER; PTHR30124; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE A; 1.
DR   PANTHER; PTHR30124:SF0; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE A; 1.
DR   Pfam; PF06725; 3D; 1.
DR   Pfam; PF03562; MltA; 1.
DR   SMART; SM00925; MltA; 1.
DR   SUPFAM; SSF50685; Barwin-like endoglucanases; 1.
PE   4: Predicted;
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Glycosidase {ECO:0000313|EMBL:EGP09395.1};
KW   Hydrolase {ECO:0000313|EMBL:EGP09395.1};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239}.
FT   DOMAIN          135..293
FT                   /note="Lytic transglycosylase MltA"
FT                   /evidence="ECO:0000259|SMART:SM00925"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          418..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          508..544
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..463
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   544 AA;  59449 MW;  A99CDE80CCD19DEF CRC64;
     MTVNAQARPA GRHHTSHGPH HELGKRAPVD WPLEIPGGQY EPLTWNEVAG WTDDDQLPAF
     KTFRASCKPI VAQKGALNDS KALGTSLRDP CLAARAENIA DSAKAREFFE KNFTPLQISR
     IGEDAGFVTG YYEPIVDGSR TQTDVYNVPV YRRPSNLFVR GYSQASASMP NKGQVFRKIG
     RRKLVPYYDR AEIEDGAIAG RGLEVVWLKS QTDLLFIQIQ GSARIRLEDG SMVRINYDAH
     NGYPYTPVGR VLIERNIVPK EQMSMQKIRE YMEQNPDAAK ELRRFNRSYV FFREVKLAAD
     DEAVGAQGVP LTAGRSIAVD KSLHVYGTPF FIEGKLPIES ETSNTPFRKL MIAQDTGSAI
     IGPARADIYF GAGAEAGRIA GRLKNPARFV MLLPNSLNPS PRGKTVPLPD ERPSATIAKL
     FPQTGPAKEA AADAPKETAK DQPKADPSKT DSSKSEQKTA PKDQPADANK TVAPKEAPAV
     QAPQVAPSAA TPSTPAAAVV PPVAQAVPLP DARPKTAPEA AAPSAVKSDT TRRSRHHRRH
     RHRR
//
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