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Database: UniProt
Entry: Q2KU19_BORA1
LinkDB: Q2KU19_BORA1
Original site: Q2KU19_BORA1 
ID   Q2KU19_BORA1            Unreviewed;       426 AA.
AC   Q2KU19;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   24-JAN-2024, entry version 86.
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   Name=mltA {ECO:0000313|EMBL:CAJ50841.1};
GN   OrderedLocusNames=BAV3231 {ECO:0000313|EMBL:CAJ50841.1};
OS   Bordetella avium (strain 197N).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910 {ECO:0000313|EMBL:CAJ50841.1, ECO:0000313|Proteomes:UP000001977};
RN   [1] {ECO:0000313|EMBL:CAJ50841.1, ECO:0000313|Proteomes:UP000001977}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=197N {ECO:0000313|EMBL:CAJ50841.1,
RC   ECO:0000313|Proteomes:UP000001977};
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA   Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA   Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA   Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT   with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT   extensive diversity in surface structures associated with host
RT   interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
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};
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DR   EMBL; AM167904; CAJ50841.1; -; Genomic_DNA.
DR   RefSeq; WP_012418868.1; NC_010645.1.
DR   AlphaFoldDB; Q2KU19; -.
DR   STRING; 360910.BAV3231; -.
DR   CAZy; GH102; Glycoside Hydrolase Family 102.
DR   GeneID; 41395065; -.
DR   KEGG; bav:BAV3231; -.
DR   eggNOG; COG2821; Bacteria.
DR   HOGENOM; CLU_037751_0_0_4; -.
DR   OMA; QRADIFY; -.
DR   OrthoDB; 9783686at2; -.
DR   Proteomes; UP000001977; 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   PIRSF; PIRSF019422; MltA; 1.
DR   SMART; SM00925; MltA; 1.
DR   SUPFAM; SSF50685; Barwin-like endoglucanases; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Glycosidase {ECO:0000313|EMBL:CAJ50841.1};
KW   Hydrolase {ECO:0000313|EMBL:CAJ50841.1};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001977};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..426
FT                   /note="peptidoglycan lytic exotransglycosylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004211939"
FT   DOMAIN          160..319
FT                   /note="Lytic transglycosylase MltA"
FT                   /evidence="ECO:0000259|SMART:SM00925"
FT   REGION          21..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   426 AA;  46266 MW;  EDC4602CCBAFC90D CRC64;
     MKRLFCLSLL SALLAACSTT SEIPPESRGP GQAVSEGPLV VPTTLPDTPP RALAGHYQRA
     AWSELPGWES DDLSRLWPLV LRNCKGLVRP ASGNLTVPAR ATPRAWQPVC AAAADPARAP
     AAGDGAAVRR FLQSYLQPWR LVGADGRVAS NTVTGYYEPL VRGSRERGGR HQWPLYGVPD
     DLLIIDLGAV YPDLAGKRVR GKLDGRRVVP YDTRAGIEAS SRKPPVVAWV DDPVDNFFLQ
     VQGSGRVQLT EGPDAGKTIR VAYADHNGQP YVSIGRWLID RGELRADQAS MQNIRAWAQR
     NPSRVQEMLN ANPAVVFFRE ETVADPEQGP KGAYGIALAA GRAIAVDPTF VPLGTPVYLS
     TTYPASERPL QRLVFAQDTG TAIKGAARAD YYWGFGDEAG QQAGRMKQRG QMWLLWPKQA
     GEPSAR
//
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