ID D0W3T7_NEICI Unreviewed; 239 AA.
AC D0W3T7;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 24-JAN-2024, entry version 45.
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=NEICINOT_04328 {ECO:0000313|EMBL:EEZ71485.1};
OS Neisseria cinerea ATCC 14685.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=546262 {ECO:0000313|EMBL:EEZ71485.1, ECO:0000313|Proteomes:UP000003294};
RN [1] {ECO:0000313|EMBL:EEZ71485.1, ECO:0000313|Proteomes:UP000003294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14685 {ECO:0000313|EMBL:EEZ71485.1,
RC ECO:0000313|Proteomes:UP000003294};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (OCT-2009) 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:EEZ71485.1}.
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DR EMBL; ACDY02000007; EEZ71485.1; -; Genomic_DNA.
DR RefSeq; WP_003676962.1; NZ_ACDY02000007.1.
DR AlphaFoldDB; D0W3T7; -.
DR STRING; 546262.NEICINOT_04328; -.
DR eggNOG; COG0797; Bacteria.
DR OrthoDB; 9779128at2; -.
DR Proteomes; UP000003294; Unassembled WGS sequence.
DR GO; GO:0008932; F:lytic endotransglycosylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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 cycle {ECO:0000313|EMBL:EEZ71485.1};
KW Cell division {ECO:0000313|EMBL:EEZ71485.1};
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 Signal {ECO:0000256|HAMAP-Rule:MF_02071}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02071"
FT CHAIN 26..239
FT /note="Endolytic peptidoglycan transglycosylase RlpA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02071"
FT /id="PRO_5009991129"
FT DOMAIN 160..239
FT /note="SPOR"
FT /evidence="ECO:0000259|PROSITE:PS51724"
SQ SEQUENCE 239 AA; 26036 MW; 90D5C4CFAFFDF3BE CRC64;
MTLTRKTLFL LTATFGIHSF QTASADAVVK AEKLHASANR SYKVAGKRYT PINQVAAFTQ
TGNASWYGGR FHGRKTSGGE RYDMNAFTAA HKTLPIPSYV RVTNTRNGKS VVVRINDRGP
FHSNRIIDVS KAAAQQLGFV SQGTAHVKIE QIVPGKSSPT AENKDIFIDL KSFGTEREAQ
AYLNHAAQNL ASSASNPNLS VEKRHYEYVV KMGPFSSQER AAEAESQARG MIQTALTAG
//
