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Database: UniProt
Entry: Q5F638_NEIG1
LinkDB: Q5F638_NEIG1
Original site: Q5F638_NEIG1 
ID   Q5F638_NEIG1            Unreviewed;       228 AA.
AC   Q5F638;
DT   15-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2005, sequence version 1.
DT   24-JAN-2024, entry version 84.
DE   RecName: Full=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=NGO_1728 {ECO:0000313|EMBL:AAW90349.1};
OS   Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90349.1, ECO:0000313|Proteomes:UP000000535};
RN   [1] {ECO:0000313|Proteomes:UP000000535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535};
RA   Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA   Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA   Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA   Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT   "The complete genome sequence of Neisseria gonorrhoeae.";
RL   Submitted (MAR-2003) 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; AE004969; AAW90349.1; -; Genomic_DNA.
DR   RefSeq; WP_003696139.1; NC_002946.2.
DR   RefSeq; YP_208761.1; NC_002946.2.
DR   AlphaFoldDB; Q5F638; -.
DR   STRING; 242231.NGO_1728; -.
DR   KEGG; ngo:NGO_1728; -.
DR   PATRIC; fig|242231.10.peg.2067; -.
DR   HOGENOM; CLU_042923_3_4_4; -.
DR   OMA; PYSALGM; -.
DR   Proteomes; UP000000535; Chromosome.
DR   GO; GO:0008932; F:lytic endotransglycosylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro.
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   InterPro; IPR007730; SPOR-like_dom.
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   Pfam; PF05036; SPOR; 1.
DR   SUPFAM; SSF50685; Barwin-like endoglucanases; 1.
DR   PROSITE; PS51724; SPOR; 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:UP000000535};
KW   Signal {ECO:0000256|HAMAP-Rule:MF_02071}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02071"
FT   CHAIN           26..228
FT                   /note="Endolytic peptidoglycan transglycosylase RlpA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02071"
FT                   /id="PRO_5009992580"
FT   DOMAIN          149..228
FT                   /note="SPOR"
FT                   /evidence="ECO:0000259|PROSITE:PS51724"
SQ   SEQUENCE   228 AA;  24694 MW;  39A12BA346DBE38A CRC64;
     MTLTRKTLFL LTAAFGTHSL QTASADAVVK PEKLHASANR SYKVAEFTQT GNASWYGGRF
     HGRKTSGGDR YDMNAFTAAH KTLPIPSHVR VTNTKNGKSV IVRVNDRGPF HGNRIIDVSK
     AAAQKLGFVS QGTAHVKIEQ IVPGQSAPVA ENKDIFIDLK SFGTEHEAQA YLNQAAQNFA
     ASSSSPNLSV EKRRYEYVVK MGPFASQERA AEAEAQARGM VRAVLTSG
//
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