ID A0A077EAK1_9FLAO Unreviewed; 134 AA.
AC A0A077EAK1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Probable endolytic peptidoglycan transglycosylase RlpA {ECO:0000256|HAMAP-Rule:MF_02071};
DE EC=4.2.2.- {ECO:0000256|HAMAP-Rule:MF_02071};
DE Flags: Precursor;
GN Name=rlpA {ECO:0000256|HAMAP-Rule:MF_02071};
GN ORFNames=BD94_0737 {ECO:0000313|EMBL:AIL44512.1};
OS Elizabethkingia anophelis NUHP1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Elizabethkingia.
OX NCBI_TaxID=1338011 {ECO:0000313|EMBL:AIL44512.1, ECO:0000313|Proteomes:UP000028933};
RN [1] {ECO:0000313|EMBL:AIL44512.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NUHP1 {ECO:0000313|EMBL:AIL44512.1};
RX PubMed=24012265; DOI=10.1016/S0140-6736(13)61858-9;
RA Teo J., Tan S.Y., Tay M., Ding Y., Kjelleberg S., Givskov M., Lin R.T.,
RA Yang L.;
RT "First case of E anophelis outbreak in an intensive-care unit.";
RL Lancet 382:855-856(2013).
RN [2] {ECO:0000313|EMBL:AIL44512.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NUHP1 {ECO:0000313|EMBL:AIL44512.1};
RX PubMed=26019164; DOI=10.1093/gbe/evv101;
RA Li Y., Liu Y., Chew S.C., Tay M., Salido M.M., Teo J., Lauro F.M.,
RA Givskov M., Yang L.;
RT "Complete Genome Sequence and Transcriptomic Analysis of the Novel Pathogen
RT Elizabethkingia anophelis in Response to Oxidative Stress.";
RL Genome Biol. Evol. 7:1676-1685(2015).
CC -!- FUNCTION: Lytic transglycosylase with a strong preference for naked
CC glycan strands that lack stem peptides. {ECO:0000256|HAMAP-
CC Rule:MF_02071}.
CC -!- SIMILARITY: Belongs to the RlpA family. {ECO:0000256|HAMAP-
CC Rule:MF_02071, ECO:0000256|RuleBase:RU003495}.
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DR EMBL; CP007547; AIL44512.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077EAK1; -.
DR STRING; 1338011.BD94_0737; -.
DR KEGG; eao:BD94_0737; -.
DR eggNOG; COG0797; Bacteria.
DR HOGENOM; CLU_042923_7_2_10; -.
DR Proteomes; UP000028933; Chromosome.
DR GO; GO:0008932; F:lytic endotransglycosylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000270; P:peptidoglycan metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd22268; DPBB_RlpA-like; 1.
DR Gene3D; 2.40.40.10; RlpA-like domain; 1.
DR HAMAP; MF_02071; RlpA; 1.
DR InterPro; IPR034718; RlpA.
DR InterPro; IPR009009; RlpA-like_DPBB.
DR InterPro; IPR036908; RlpA-like_sf.
DR InterPro; IPR012997; RplA.
DR NCBIfam; TIGR00413; rlpA; 1.
DR PANTHER; PTHR34183; -; 1.
DR PANTHER; PTHR34183:SF1; ENDOLYTIC PEPTIDOGLYCAN TRANSGLYCOSYLASE RLPA; 1.
DR Pfam; PF03330; DPBB_1; 1.
DR SUPFAM; SSF50685; Barwin-like endoglucanases; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|HAMAP-Rule:MF_02071};
KW Lipoprotein {ECO:0000313|EMBL:AIL44512.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_02071};
KW Signal {ECO:0000256|HAMAP-Rule:MF_02071}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02071"
FT CHAIN 29..134
FT /note="Probable endolytic peptidoglycan transglycosylase
FT RlpA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02071"
FT /id="PRO_5009982515"
FT DOMAIN 46..130
FT /note="RlpA-like protein double-psi beta-barrel"
FT /evidence="ECO:0000259|Pfam:PF03330"
SQ SEQUENCE 134 AA; 14808 MW; F2D2D98D7A89AB14 CRC64;
MLIFGFYMKL IKRMSRVIFL LTLLPAIACS TVSNMKSGEE KSTTVSYYSD TFNGRKTSSG
EVFDNGKLTA AHANLPFGTK VLLTNVATGD TVTVKVNDRG YLHKGRAFDI TKSAFKKLGD
VRKGVLKVTY RVLE
//
