ID A0A2S6CR24_9CYAN Unreviewed; 409 AA.
AC A0A2S6CR24;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
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};
GN Name=rlpA {ECO:0000256|HAMAP-Rule:MF_02071};
GN ORFNames=CUN59_17400 {ECO:0000313|EMBL:PPJ62070.1};
OS Cuspidothrix issatschenkoi CHARLIE-1.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC Cuspidothrix.
OX NCBI_TaxID=2052836 {ECO:0000313|EMBL:PPJ62070.1, ECO:0000313|Proteomes:UP000239589};
RN [1] {ECO:0000313|EMBL:PPJ62070.1, ECO:0000313|Proteomes:UP000239589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHARLIE-1 {ECO:0000313|EMBL:PPJ62070.1,
RC ECO:0000313|Proteomes:UP000239589};
RA Kust A., Mares J., Jokela J., Urajova P., Hajek J., Saurav K., Voracova K.,
RA Fewer D.P., Haapaniemi E., Permi P., Rehakova K., Sivonen K., Hrouzek P.;
RT "Discovery of a pederin family compound in a non-symbiotic bloom-forming
RT cyanobacterium.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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:PPJ62070.1}.
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DR EMBL; PGEM01000143; PPJ62070.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S6CR24; -.
DR OrthoDB; 9779128at2; -.
DR Proteomes; UP000239589; Unassembled WGS sequence.
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 Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_02071};
KW Reference proteome {ECO:0000313|Proteomes:UP000239589}.
FT DOMAIN 287..373
FT /note="RlpA-like protein double-psi beta-barrel"
FT /evidence="ECO:0000259|Pfam:PF03330"
SQ SEQUENCE 409 AA; 45210 MW; 88366321363AE1E8 CRC64;
MISIVMLGVA SLMDGTLMLT RNLPTGVIAK VSPTQFTNNL EKTQAEFFSI AKAYKRIWSK
NLVLTNLFPF NGKSRELASA VNTVNSSIST TLTAKETELC AYVPENIAAQ SQLQNATHSL
PAPVSQISFP KINISPANVV RSLESFFKAI NNPLEQNSSH DYAPVLIVRR NYYNYEVWVN
NSFVARLPDQ ITANFLKERL QQLVSSPTIQ PTQLQPGLVD NTPSLMVGNR LLFAINRQLS
NQLGSNGHTL AIQWINNLRI ALHAEPLTLV QGQIEIYGLE SSTTKLSGLA SWYGGYFHGR
LTANGEIYNQ DDFTVAHRSL PFNTYLKVTN TKNGKSVIVR VNDRGPYISP RSLDLSRTAA
RCLGSEHTGV VPYQAVVLQQ NAPQMTLNPS PVKTQEMANA KSELLVSKF
//
