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Database: UniProt
Entry: A0A7U3ZIN1_RUNSL
LinkDB: A0A7U3ZIN1_RUNSL
Original site: A0A7U3ZIN1_RUNSL 
ID   A0A7U3ZIN1_RUNSL        Unreviewed;       773 AA.
AC   A0A7U3ZIN1;
DT   02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 1.
DT   18-JUN-2025, entry version 19.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00044770};
DE            EC=2.4.99.28 {ECO:0000256|ARBA:ARBA00044770};
GN   OrderedLocusNames=Runsl_1504 {ECO:0000313|EMBL:AEI47929.1};
OS   Runella slithyformis (strain ATCC 29530 / DSM 19594 / LMG 11500 / NCIMB
OS   11436 / LSU 4).
OC   Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
OC   Spirosomataceae; Runella.
OX   NCBI_TaxID=761193 {ECO:0000313|EMBL:AEI47929.1, ECO:0000313|Proteomes:UP000000493};
RN   [1] {ECO:0000313|Proteomes:UP000000493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29530 / DSM 19594 / LMG 11500 / NCIMB 11436 / LSU 4
RC   {ECO:0000313|Proteomes:UP000000493};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., Zhang X.,
RA   Misra M., Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Faehrich R.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of chromosome of Runella slithyformis DSM 19594.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEI47929.1, ECO:0000313|Proteomes:UP000000493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29530 / DSM 19594 / LMG 11500 / NCIMB 11436 / LSU 4
RC   {ECO:0000313|Proteomes:UP000000493};
RX   PubMed=22768358; DOI=10.4056/sigs.2475579;
RA   Copeland A., Zhang X., Misra M., Lapidus A., Nolan M., Lucas S.,
RA   Deshpande S., Cheng J.F., Tapia R., Goodwin L.A., Pitluck S., Liolios K.,
RA   Pagani I., Ivanova N., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Pan C., Jeffries C.D., Detter J.C., Brambilla E.M.,
RA   Rohde M., Djao O.D., Goker M., Sikorski J., Tindall B.J., Woyke T.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P., Mavromatis K.;
RT   "Complete genome sequence of the aquatic bacterium Runella slithyformis
RT   type strain (LSU 4(T)).";
RL   Stand. Genomic Sci. 6:145-154(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC         Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC         (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC         cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC         D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans,octa-cis-undecaprenyl
CC         diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC         Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC         ChEBI:CHEBI:78435; EC=2.4.99.28;
CC         Evidence={ECO:0000256|ARBA:ARBA00049902};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC       family. {ECO:0000256|ARBA:ARBA00007090}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       glycosyltransferase 51 family. {ECO:0000256|ARBA:ARBA00007739}.
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DR   EMBL; CP002859; AEI47929.1; -; Genomic_DNA.
DR   RefSeq; WP_013927245.1; NC_015703.1.
DR   AlphaFoldDB; A0A7U3ZIN1; -.
DR   KEGG; rsi:Runsl_1504; -.
DR   Proteomes; UP000000493; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:TreeGrafter.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:InterPro.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:InterPro.
DR   GO; GO:0006793; P:phosphorus metabolic process; IEA:UniProtKB-ARBA.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR001264; Glyco_trans_51.
DR   InterPro; IPR050396; Glycosyltr_51/Transpeptidase.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR011815; PBP_1c.
DR   InterPro; IPR009647; PBP_C.
DR   InterPro; IPR036950; PBP_transglycosylase.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   NCBIfam; TIGR02073; PBP_1c; 1.
DR   PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR32282:SF15; PENICILLIN-BINDING PROTEIN 1C; 1.
DR   Pfam; PF06832; BiPBP_C; 1.
DR   Pfam; PF00912; Transgly; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   PROSITE; PS50035; PLD; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000313|EMBL:AEI47929.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000493};
KW   Transferase {ECO:0000313|EMBL:AEI47929.1}.
FT   DOMAIN          303..334
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
SQ   SEQUENCE   773 AA;  87330 MW;  589DEF1A1002D3DF CRC64;
     MEKRRQKAFN VLKKWLRSRR FWLLASPFLL FIVLDAALPF KVAPSYSTLV VAADGTILHA
     FLNDHDKWRL YTEPDEITPL LRQTILQKED RFFYFHPGFN PIALGRALVK NTVTGRRSSG
     ASTITMQVVR LLEPRKRTYL SKGIELFRAM QLELHYSKDE ILQLYLNLIP YGSNIEGMKS
     ASLLYFGKLP QLLSLAEITT LTIIPNRPSS LRLGRKNTFI VQERNKWLKR FERDGLFDKQ
     IIADAINEPL NAYRREAPKW VPHLAFRLKN EQKNTPIIRT AILPTRQAQV EQMTRNYVNR
     LQSMNIHNAA VMVINNETMQ VETYVGSADF NNSYDGGQVD GIKAIRSPGS TLKPLLYAIA
     FDKGMITPKS AVNDVPTNFG GFEPENFDRR FNGKVSIEFA LANSLNIPAV KVLKDMTPGV
     LINYLKKADF QTVKKQSKDL GLSMILGGCG VTLEELTRLF TAFANDGKMH GLNYTKEAEK
     AKGEVLISPE SAYLITTILT QITRPDLPNN FDNTYHLPRI AWKTGTSYGK KDAWSIGYNR
     RYTVGVWVGN FSGMGVPELN GANIATPLLF DVFNAIDYNS PTGWFKPAAD ITRRKVCAES
     GDLPAEFCTH QVLDYAIMGI SPTRRCQHLK WVLTDQTAKI SYCTQCLPDS GYVRKLYINL
     APGLIAYNEL NRIPYQRIPP HNPNCTRVFD IGAPIITSPN DGSEYFLEGQ QLQLACQAAN
     DVREVYWYVN DKLVQKANPQ AALFIKPPVG KVKISCSDDK GRNADVFINV LTQ
//
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