ID K9Z9D0_ANACC Unreviewed; 366 AA.
AC K9Z9D0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
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 OrderedLocusNames=Anacy_0163 {ECO:0000313|EMBL:AFZ55771.1};
OS Anabaena cylindrica (strain ATCC 27899 / PCC 7122).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Anabaena.
OX NCBI_TaxID=272123 {ECO:0000313|EMBL:AFZ55771.1, ECO:0000313|Proteomes:UP000010474};
RN [1] {ECO:0000313|Proteomes:UP000010474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27899 / PCC 7122 {ECO:0000313|Proteomes:UP000010474};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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; CP003659; AFZ55771.1; -; Genomic_DNA.
DR RefSeq; WP_015212427.1; NZ_AP018166.1.
DR AlphaFoldDB; K9Z9D0; -.
DR STRING; 272123.Anacy_0163; -.
DR KEGG; acy:Anacy_0163; -.
DR PATRIC; fig|272123.3.peg.175; -.
DR eggNOG; COG0797; Bacteria.
DR HOGENOM; CLU_042923_0_0_3; -.
DR OrthoDB; 9779128at2; -.
DR Proteomes; UP000010474; 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:AFZ55771.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_02071};
KW Reference proteome {ECO:0000313|Proteomes:UP000010474}.
FT DOMAIN 273..361
FT /note="RlpA-like protein double-psi beta-barrel"
FT /evidence="ECO:0000259|Pfam:PF03330"
SQ SEQUENCE 366 AA; 39164 MW; 92C3E719ED79EC80 CRC64;
MNQRHLWTTA ALFLTVLGTP SVGLTQTTEE NTPTSPASAL TDVVKVGEYQ SPAQKPTLDA
VKTDIHPHSI GGRQAATLYI RNIPVLTFLS SAPVTSAETK VGAVANGNGV KSYALVSNNS
AKVASIGNVI DVSKSPSSIA DDPVQRASVV AARINQLIDE NVDASQITVS WKTTEQSPVN
NKAQDKTHSV KQQLDRYTIK VDGQELVEIN QGTQLADSTK DLARDALQAT NRLRRLIGNA
SPISEIANLP VSTPALTSKL PQQIARGFKI NFQGIASWYG YDWAGRKTAN GERFNPDAMT
AAHRSLPMGT QVRVTNTRNN RSVVVRINDR GPYIGGRIID VSIGAARLLG MVGSGVAPVR
IDILGR
//
