ID   A0A1Z4RC82_9CYAN        Unreviewed;       378 AA.
AC   A0A1Z4RC82;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=NIES4101_60390 {ECO:0000313|EMBL:BAZ40078.1};
OS   Calothrix sp. NIES-4101.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC   Calothrix.
OX   NCBI_TaxID=2005461 {ECO:0000313|EMBL:BAZ40078.1, ECO:0000313|Proteomes:UP000290974};
RN   [1] {ECO:0000313|EMBL:BAZ40078.1, ECO:0000313|Proteomes:UP000290974}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-4101 {ECO:0000313|EMBL:BAZ40078.1,
RC   ECO:0000313|Proteomes:UP000290974};
RA   Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT   "Genome sequencing of cyanobaciteial culture collection at National
RT   Institute for Environmental Studies (NIES).";
RL   Submitted (JUN-2017) 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}.
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DR   EMBL; AP018280; BAZ40078.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z4RC82; -.
DR   Proteomes; UP000290974; 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:BAZ40078.1};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_02071};
KW   Reference proteome {ECO:0000313|Proteomes:UP000290974};
KW   Signal {ECO:0000256|HAMAP-Rule:MF_02071}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02071"
FT   CHAIN           24..378
FT                   /note="Probable endolytic peptidoglycan transglycosylase
FT                   RlpA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02071"
FT                   /id="PRO_5013416551"
FT   DOMAIN          285..373
FT                   /note="RlpA-like protein double-psi beta-barrel"
FT                   /evidence="ECO:0000259|Pfam:PF03330"
SQ   SEQUENCE   378 AA;  40130 MW;  4097E7A1CBB2F7CC CRC64;
     MNHRYFLTVF ALLSAFVGSP SIARSQTTAQ SNSTLPSSPS GDVVKVGEYQ TKTDTPAARN
     AVTQIHTHNK AGRQAATLYI RNIPVLTFVG KQQVASTDSK TETKVGAIGN VGGENGGVQQ
     YAPNASNSSS VKVATVGENA GLANQVNLSN DDPVQKASIV AARINDLVRQ KVDANKITVS
     WRRGGEVATA NQAGNKNLSN QESEARYVIK VDGQEIVAID SNTSLSDSTN NQAQDALQAT
     NRLRRLIGNA SPLTEIANLP VNVPAISIPK SPDQIAIAPV KQVLNGIASF YGYDGSGNKT
     ATGERFNPEG MTAAHRHLPF GTRVRVTNIR NGRSVIVRIN DRGPFIRGRI IDLSYGAARV
     IGMIGRGIAP VKVEVLGR
//